Milk taste can be enhanced by new LED display lights

New LED lights are known to reduce the energy bills across the globe but little did we know that they also help milk taste fresh, sweet and rich.

Remember the freshly pasteurized milk our grandparent's used to receive at their doorstep? It used to be so yummy. But we don't fall the same way for the milk that has been exposed to conventional fluorescent lights. Milk is delicious and nutritious but its consumption has been decreasing for several decades. This concern made the researchers at Virginia Tech to find ways to protect the milk characteristics to help the industry and to provide consumers the better and rich product. 

Researchers on conducting a series of experiments found that new LED lights positioned in milk display cabinets does help milk retaining its fresh taste but packaging should also be taken into consideration to get the fresh milk taste. Riboflavin, one of the nutrients in milk, oxidizes on exposure to fluorescent lights. This oxidation reaction changes the milk taste as well as reduces the nutritional value of the milk. Therefore, opaque milk packaging will also help to deliver milk with fresh and rich taste. 

This new lighting research has given the impetus to researchers to explore other ways to protect the natural taste of milk.  

Estimation of Dissolved oxygen (DO) in a water sample

Dissolved oxygen content in a water sample is indicative of its quality. Amount of dissolved oxygen in the water of river, pond, etc., determines whether biological flora and fauna, other aquatic living organisms viz. fishes will survive in it or not. Dissolved oxygen is also determined in waste water/ industrial effluent since it is an index of its pollution. Although nowadays, more sensitive methods like electrodes are available, still titrimetric method is in common use.  It is generally defined as number of milli-litres of oxygen gas per litre of water (ml. L^-1).

Principle:

The estimation of dissolved oxygen is done using titrimetric method. In the alkaline condition, manganese sulfate gets converted into manganous hydroxide. The oxygen present in the liquid combines with manganous hydroxide and oxidizes manganese to tetravalent state, MnO(OH)₂, and this MnO(OH)₂ on acidification liberates iodine equivalent to that of oxygen fixed. The liberated iodine is titrated using standard sodium thiosulfate solution and starch as indicator.

Sodium thiosulfate upon reaction with iodine forms sodium tetrathionate and sodium iodide. Here, progress of the reaction is monitored by using starch as indicator since starch after binding iodine gives blue colored complex.

2Na₂S₂O₃ + I₂ ==== Na₂S₄O₆ + 2NaI 

Reagents:

Sodium thiosulfate (N/40): Weigh 6.20 gm of sodium thiosulfate (Na2S2O3.5H2O), dissolve in water and make the volume 1 litre.  

Manganous sulfate (48%): Weigh 48 gm of manganous sulfate and dissolve in 100 ml of water.

Potassium iodide (15%) in potassium hydroxide (KOH) (70%): Prepare 70% KOH by dissolving 70 gm of KOH in 100 ml of water. Thereafter, weigh 15 gm of potassium iodide and dissolve in 70% KOH and make the volume 100 ml using 70% KOH.

Starch indicator (1%): Weigh 1 gm of soluble starch, add water and dissolve by gentle heating. Make the volume 100 ml using water.

Sulfuric acid (36N): Use commercial analytical grade sulfuric acid of 36 normality.

Protocol:

1. Pipette known volume of the liquid sample in a 250 ml glass bottle avoiding bubbles.

2. Add 2 ml each of manganous sulfate and alkaline potassium iodide solution in succession right at the bottom of the bottle using separate pipets and thereafter replace the stopper.

3. Shake the bottle well and allow the brown precipitate formed to settle. This brown precipitate is of MnO(OH)₂.

4. Add 2 ml of concentrated sulfuric acid and shake well to dissolve the brown precipitate.

5. Titrate the liberated iodine against standard sodium thiosulfate using starch as an indicator. At the end point, blue color will disappear.

If we check the stoichiometry of the reactions, one mole of oxygen will be equivalent to 2 moles of iodine.

After calculating the number of moles of iodine produced, calculate the number of moles of oxygen present in the sample. The dissolved oxygen content is generally expressed as mg/100 ml sample.

Source:

‘Biochemical Tests: Principles and Protocols’, Viva Books Pvt Ltd, New Delhi, India, 2012.

Frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17)

By Sarika Garg

FTDP-17 is a group of familial neurodegenerative Tauopathies characterized by diverse but overlapping clinical and neuropathologic features. According to several reports on clinical and neuropathologic features of FTDP-17, three major clinical syndromes have been delineated. These syndromes are disinhibition-dementia-parkinsonism-amyotrophy complex (DDPAC), pallid-ponto-nigral degeneration (PPND), and familial multiple system tauopathy with presenile dementia (MSTD). The clinical characteristics of these FTDP-17 Tauopathies variably include memory and language impairments, behavioral and psychiatric abnormalities, extrapyramidal signs, and motor deficits. However, all FTDP-17 brains from affected patients share a common neuropathology characterized by abundant neuronal and to a lesser extent glial fibrillary lesions composed of hyperphosphorylated Tau proteins and are associated with a remarkable loss of neurons in affected regions. 

Autosomal dominant inheritance of these FTDP-17 syndromes suggested that one or more genetic mutations might be pathogenic for these disorders, and linkage analyses showed co-segregation of disease with a genetic locus on chromosome 17q21.1. Since pathologic hallmarks of these disorders are Tau lesions and Tau gene resides within the disease locus of chromosome 17, Tau gene is an obvious candidate for pathogenic mutations in FTDP-17 kindreds. More than 40 different mutations in Tau gene are known to occur in FTDP-17.

Fig.: Tau mutations that result in frontotemporal dementia and parkinsonism linked to chromosome-17 (FTDP-17) map primarily to exons 9-12 or to the intronic region between exons 10 and 11.

In FTDP-17, two mechanisms have been proposed to mediate the effects of mutations in Tau gene. The first mechanism involves perturbations of the alternative splicing of exon 10 resulting change in the ratio of 4R:3R Tau. These mutations comprise a mixture of coding changes, within exon 10 (N279K, delK280, L284L, N296N/H, delN296, P301L/S, G303V, and S305S/N) and also intronic mutations close to the 5’ splice site of exon 10 (at positions +3, +11, +12, +13, +14, +16, +19, and +29). The second mechanism suggests that coding mutations (missense and deletions) directly cause deficits in the abilities of Tau to bind with microtubules (MTs) and promote assembly and stability of MTs. This has been linked to several Tau gene missense mutations including: G272V, delK280, P301L, P301S, V337M, G389R, and R406W using in vitro studies. Tau filaments formation is enhanced by heparin using recombinant G272V, P301L, V337M, and R406W mutant Tau proteins compared to wild type Tau protein. Moreover, mutations in exons other than those in exon 10 (V337M and R406W) promote Tau aggregation which is composed of all six isoforms, whereas other exon 10 mutations (P301L) increase 4R Tau in insoluble FTDP-17 brain fractions. Mutations in the intronic sequence adjacent to the stem loop structure in exon 10 have been identified that alter Tau splicing to increase soluble 3R Tau, leading to increased Tau proteolysis and neuronal apoptosis without deposition of insoluble Tau aggregates.

References:

Arrasate, M., Pérez, M., Armas-Portela, R., Avila, J., 1999. Polymerization of Tau peptides into fibrillar structures. The effect of FTDP-17 mutations. FEBS Lett. 446(1), 199-202.

Clark, L.N., Poorkaj, P., Wszolek, Z., Geschwind, D.H., Nasreddine, Z.S., Miller, B., Li, D., Payami, H., Awert, F., Markopoulou, K., Andreadis, A., D'Souza, I., Lee, V.M., Reed, L., Trojanowski, J.Q., Zhukareva, V., Bird, T., Schellenberg, G., Wilhelmsen, K.C., 1998. Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17. Proc Natl Acad Sci USA. 95(22), 13103-13107.

Foster, N.L., Wilhelmsen, K., Sima, A.A., Jones, M.Z., D'Amato, C.J., Gilman, S., 1997. Frontotemporal dementia and parkinsonism linked to chromosome 17: a consensus conference. Conference Participants. Ann Neurol. 41(6), 706-715.

Goedert, M., Spillantini, M.G. , 2001. Tau gene mutations and neurodegeneration. Biochem Soc Symp. 67, 59-71.

Hong, M., Zhukareva, V., Vogelsberg-Ragaglia, V., Wszolek, Z., Reed, L., Miller, B.I., Geschwind, D.H., Bird, T.D., McKeel, D., Goate, A., Morris, J.C., Wilhelmsen, K.C., Schellenberg, G.D., Trojanowski, J.Q., Lee, V.M., 1998. Mutation-specific functional impairments in distinct Tau isoforms of hereditary FTDP-17. Science. 282(5395), 1914-1917.

Lynch, T., Sano, M., Marder, K.S., Bell, K.L., Foster, N.L., Defendini, R.F., Sima, A.A., Keohane, C., Nygaard, T.G., Fahn, S., et al., 1994. Clinical characteristics of a family with chromosome 17-linked disinhibition-dementia-parkinsonism-amyotrophy complex. Neurology. 44(10), 1878-1884.

Reed, L.A., Schmidt, M.L., Wszolek, Z.K., Balin, B.J., Soontornniyomkij, V., Lee, V.M., Trojanowski, J.Q., Schelper, R.L., 1998. The neuropathology of a chromosome 17-linked autosomal dominant parkinsonism and dementia ("pallido-ponto-nigral degeneration"). J Neuropathol Exp Neurol. 57(6), 588-601.

Schneider, A., Mandelkow, E., 2008. Tau-based treatment strategies in neurodegenerative diseases. Neurotherapeutics. 5, 443-457.

Spillantini, M.G., Goedert, M., Crowther, R.A., Murrell, J.R., Farlow, M.R., Ghetti, B., 1997. Familial multiple system Tauopathy with presenile dementia: a disease with abundant neuronal and glial Tau filaments. Proc Natl Acad Sci USA. 94(8), 4113-4118.

Stanford, P.M., Shepherd, C.E., Halliday, G.M., Brooks, W.S., Schofield, P.W., Brodaty, H., Martins, R.N., Kwok, J.B., Schofield, P.R., 2003. Mutations in the Tau gene that cause an increase in three repeat Tau and frontotemporal dementia. Brain. 126(Pt 4), 814-826.

Wijker, M., Wszolek, Z.K., Wolters, E.C., Rooimans, M.A., Pals, G., Pfeiffer, R.F., Lynch, T., Rodnitzky, R.L., Wilhelmsen, K.C., Arwert, F., 1996. Localization of the gene for rapidly progressive autosomal dominant parkinsonism and dementia with pallido-ponto-nigral degeneration to chromosome 17q21. Hum Mol Genet. 5(1), 151-154. 

Copyright © 2017 HS Counseling. All rights reserved. 

Alzheimer’s Disease

By Sarika Garg

Alzheimer’s disease (AD) is named after German psychiatrist and pathologist Dr. Alois Alzheimer. In 1907, he published an account of a 51-years old female patient, Auguste D from Frankfurt, who suffered from strong feelings of jealousy towards her husband, increased memory impairment, disorientation, hallucinations, and often loud and aggressive behaviour. After four and a half years of rapidly deteriorating mental illness, Auguste D died in a completely demented state. Postmortem histological analysis of her brain using the Bielschowsky silver technique revealed dense bundles of unusual fibrils within nerve cells (neurofibrillary tangles or NFTs) and numerous focal lesions within the cerebral cortex, subsequently named as ’’senile plaques’’.

Alzheimer’s disease is a devastating neurodegenerative disorder. It is an irreversible, progressive and fatal brain disease. It is neither infectious nor contagious, but it is the single most common form of dementia, a term used to describe a general decline in all areas of mental ability. The symptoms are deterioration in cognitive processes- memory, language, thinking and so on- with important repercussions on behaviour. About 50 per cent of the people with dementia suffer from Alzheimer’s disease, about 20 per cent from vascular dementia (caused by blockages in the supply of blood to the brain), and about 20 per cent from Lewy body dementia (characterized by tiny spherical deposits in the brain). The risk of getting Alzheimer’s disease increases as one gets older (beyond age 65). By age 85, about 35 out of 100 people have some form of dementia. Alzheimer’s disease is the ninth leading cause of death. It is estimated that more than 60 per cent of people with dementia live in developing countries, however, by 2040, it is expected to rise by 71 per cent.

Studies have supported the notion that 70 to 80% of the risk to develop Alzheimer’s disease is determined by genetic factors. Alzheimer’s disease is not a single-gene disorder. Genetically, Alzheimer’s disease (AD) is a complex and heterogeneous disease involving mutations and polymorphisms in multiple genes on several chromosomes. The two basic types of Alzheimer’s disease are: the late sporadic AD (SAD) and the early familial AD (FAD). The SAD represents the vast majority of cases whose aging itself is the unique important risk factor known. The apolipoprotein E (APOE) gene located on chromosome 19q13.2 has been confirmed unequivocally as a risk gene. Its ε4 allele increases the susceptibility to SAD whereas its ε2 allele confers protection against the late onset of AD. Besides cases arising sporadically, epidemiological studies indicate that about 30% of AD patients have a family history of disease and at least one first-degree relative is affected, however, only a few of them have a clear autosomal dominant inheritance. The FAD starts before 60 and accounts for less than 1% of the total number of AD cases. It is associated with gene mutations on chromosomes 1, 14, and 21. Only 5% of the amyloid precursor protein (APP) mutations have been estimated for FAD. Most of the FAD cases are caused by mutations in two genes namely presenelin 1 (PSEN1) and presenelin 2 (PSEN2). In AD, no mutation has been identified in the gene, MAPT which codes for Tau protein. However, more than 40 exonic and intronic mutations in MAPT present on chromosome 17q21.1, have been found in a familial dementia related to AD, and in the frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17).   

The actual causes of Alzheimer’s disease are not yet known with certainty. Alzheimer’s disease is not related to problems of the circulatory system. However, pathologically, Alzheimer’s disease is a progressive neurodegenerative disorder characterized by two main types of protein aggregation, intracellular neurofibrillary tangles (NFTs) and extracellular senile plaques (SPs). The NFTs consist of paired helical filaments (PHF) resulting from the hyper-phosphorylation of the microtubule-binding protein Tau. Senile plaques are principally composed of extracellular amyloid-ß (Aß) depositions. The amyloid cascade hypothesis posits that Aß triggers Tau pathology, but details of this relationship are poorly understood. However, there has been surprisingly scant attention focused on Tau as a therapeutic target. Advances in generating animal models with Tau pathology are helping to erase this deficit.

Fig.: Pathological hallmarks of Alzheimer’s disease. Extracellular plaques contain deposits of a protein fragment called ß-amyloid and tangles are twisted fibers of protein called Tau. Plaques build up between nerve cells and tangles form inside dying cells. The plaques and tangles tend to form in a predictable pattern, beginning in areas important in learning and memory and then spreading to other regions. The plaques and tangles contribute to the degradation of the neurons in the brain and is a central feature associated with Alzheimer’s disease.

References:

http://www.ahaf.org/alzheimers/about/understanding/plaques-and-tangles.html

Alzheimer, A., Stelzmann, R.A., Schnitzlein, H.N., Murtagh, F.R., 1907. Uber eine eigenartige Erkankung der Hirnrinde. Allg Zschr f Psychiatr Psychisch-Gerichtl Mediz. 64, 146-148.

Beers, M. H., Jones, T. V., 2004. The Merck manual of health & aging. Whitehouse Station, NJ: Merck Research Laboratories.

Bertram, L., Tanzi, R.E., 2005. The genetic epidemiology of neurodegenerative disease. J Clin Invest. 115(6), 1449-1457.

Braak, H., Braak, E., 1997. Diagnostic criteria for neuropathologic assessment of Alzheimer’s disease. Neurobiol Aging. 18, S85-S88.

Delacourte, A., Sergeant, N., Champain, D., Wattez, A., Maurage, C.A., Lebert, F., Pasquier, F., David, J.P., 2002. Nonoverlapping but synergetic Tau and APP pathologies in sporadic Alzheimer's disease. Neurology. 59(3), 398-407.

Gatz, M., Pedersen, N.L., Berg, S., Johansson, B., Johansson, K., Mortimer, J.A., Posner, S.F., Viitanen, M., Winblad, B., Ahlbom, A., 1997. Heritability for Alzheimer's disease: the study of dementia in Swedish twins. J Gerontol A Biol Sci Med Sci. 52(2), M117-M125.

Giacobini, E., 2000. Cholinesterase inhibitors stabilize Alzheimer's disease. Ann N Y Acad Sci. 920, 321-327.

Glenner, G.G., Wong, C.W., 1984. Alzheimer’s disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun. 120(3), 885-890.

Haass, C., Selkoe, D.J., 2007. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nat Rev Mol Cell Biol. 8, 101-112.

Hardy, J., Selkoe, D.J., 2002. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356.

Mandelkow, E.M., Mandelkow, E., 1998. Tau in Alzheimer’s disease. Trends Cell Biol. 8, 425-427.

McGowan, E., Eriksen, J., Hutton, M., 2006. A decade of modeling Alzheimer's disease in transgenic mice. Trends Genet. 22(5), 281-289.

Simchowicz, T., 1911. Histologische studien uber der senile demenz. Nissl-Alzheimer Histologische histopathologische. Arbeiten. 4(2), 267-444.

Sherrington, R., Rogaev, E.I., Liang, Y., Rogaeva, E.A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al., 1995. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 375(6534), 754-760.

Tanzi, R.E., 1999. A genetic dichotomy model for the inheritance of Alzheimer's disease and common age-related disorders. J Clin Invest. 104(9), 1175-1179.

Waldemar, G., Dubois, B., Emre, M., Georges, J., McKeith, I.G., Rossor, M., Scheltens, P., Tariska, P., Winblad, P., 2007. Recommendations for the diagnosis and management of Alzheimer's disease and other disorders associated with dementia: EFNS guideline. Eur J Neurol. 14(1), e1-e26.

Copyright © 2017 HS Counseling. All rights reserved. 

Tips to be ahead of the pack in exams

Scoring high marks in the class doesn’t require one to study arduously or to become a dork. Some students study hard but still don’t manage to score higher than the mates who as a matter of fact haven’t burnt the midnight oil. On the day of grades’ announcement, a bunch of average scorers stare at a high scorer pal and whisper ‘lucky dude, he is a born intelligent’. However, unbeknownst to them ‘Geniuses are not always born – they can be made too’.

Research suggests that our brain is extraordinary malleable and it can be reformed in response to our lifestyle, physiology and environment. Reforming the brain concept is called as neuroplasticity. Similar to the DNA views, it was a myth that brain is static, but today we know that we have much more control over our body and brain than we thought. Brain has an astonishing ability to rewire itself in response to experience. Flexing grey matter can bring the best out of our brain cells. This can be achieved by lots of tips, changes to our way of living, selection of food and behavior. Some of them are as follows:

Smart drugs

Smart drugs are the supplements that are known to ameliorate cognitive function as well as overall brain health.  These drugs hold the promise of improving one’s ability to learn, consolidate memories, reasoning, judgement and concentration. Some drugs are already on the block and many others are on the move.  Apex GPA is one of the obtainable supplements and is composed of natural ingredients viz. Caffeine, Panax Ginseng and Ginkgo Biloba. It is certified by Health Canada and it appreciably improves memory, alertness and intellectual performances if tucked in as per the recommendation.

Physical training

Exercise has the ability to reduce insulin resistance, inflammation and stimulate the release of growth factors in the brain. This helps in the growth and survival of new brain cells. Exercise can also increase the blood flow to the whole body, including brain. This might help you recalling your memories down the line. Recommended workout session is at least 150 minutes a week of moderate aerobic activity or 75 minutes a week of vigorous aerobic activity. However, exam days are too occupied leaving almost no time and energy for workout; therefore, squeezing in short 10 minute walks per day is also beneficial. Happy walking!

Good sleep

When the exams are nearby, students often give up their sleep to have more time to study. But walking dead in the morning is not worth without a proper brain function. A growing body of scientific evidence suggests that having requisite sleep is certainly pivotal for proper brain function, concentration, response time and to stabilize your memories. Seven to nine hours of sleep per day for an adult is adequate. Sleep tight!

Although ‘Exams’ haunt majority of the students, it’s an integral component of every student’s life. The above mentioned tips along with the positive attitude and confidence will definitely go a long way in helping you overcome the exam fever. Good luck fellas!

Source: https://www.apexgpa.com/tips-to-be-ahead-of-the-pack-exams/

Good news for milk chocolate admirers!

We all know the fact that dark chocolate is healthier than the milk one. But still most of us like to have a sweeter one and not the bitter one. Our craving lets us forget that milk chocolate lacks most of the natural and healthy antioxidants as they are lost during the making process. But soon we may not have to worry about the nutrition value of our favorite milk chocolate, all thanks to our researchers. Researchers at North Carolina State University in Raleigh found that peanut skins can be used to give the milk chocolate the same nutritional benefits as the dark chocolate. Moreover, this secret ingredient won't have any affect on the mind blowing taste.

Best things happen by chance.

Researchers didn’t start their study with the aim of finding a secret ingredient for the milk chocolate. In the United States, most peanut skins are frittered away while peanuts are used in making peanut butter. They were interested in finding a way to make good use of the wasted peanut skins.

They planned to extract antioxidants from the peanut skins. An antioxidant is a substance that inhibits the oxidation of other molecules. Studies have shown that antioxidant rich foods have a low risk of heart disease. However, antioxidants may impart a perceptible bitter taste to foods. Therefore, to disguise the bitter taste, they decided to mix the peanut skin extracts with the maltodextrin. Maltodextrin is a white powder made from corn, rice, potato starch or wheat and is used as a food additive.

Post the preparation of the antioxidant mixture, researchers added it to the milk chocolate. This addition brought the antioxidant levels in the milk chocolate equal to that of a dark chocolate without having hampered the taste of a candy.

This finding doesn’t indicate that one should turn chocolate into a staple food. Chocolate does contain fat and sugar and should not be consumed in large quantities. 

Reference:
L.L. Dean ​et​ ​al., 2016.​ ​Minimizing the negative flavor attributes and evaluating consumer acceptance of chocolate fortified with peanut skin extracts.​ ​​Journal of Food Science.​ ​​​81, ​S2824-S2830. 

Proteases

By Sarika Garg

Proteases are divided into five different groups, depending upon the type of molecule in the groove that carries out the actual work of catalysis. Serine proteases attack the peptide bond of the substrate using the hydroxyl group of the side chain of serine present in the catalytic centre. Threonine proteases act in the similar way. Cysteine proteases use the sulphur-hydrogen bond of a cysteine residue to initiate cleavage of the peptide bond. The acidic carboxyl groups of two aspartyl residues carry out this function in aspartyl proteases. Finally metalloproteases have a tightly bound zinc atom in their catalytic centre. Each of these groups of proteins is specialized to perform certain functions. For example, the coagulation of blood is the responsibility of serine proteases, whereas threonine proteases are essential, in particular, for the functioning of the proteasome, a large barrel-shaped protein-degrading apparatus in the cell. Programmed cell death is brought about by cysteine proteases. Digestion can not occur without aspartyl proteases and a subgroup of metalloproteases is essential for the breakdown and rebuilding of the extracellular matrix.

Proteases do not attack their protein substrates at random. Rather, they display a high degree of specificity. This specificity is not defined by the nature of the catalytic centre alone. On either side of the catalytic centre, there is a series of binding sites that favour particular amino acid in the substrate.    

Fig.: Specificity of protease binding. The specificity of protease binding is not defined solely by the nature of the catalytic centre. On either side of the catalytic centre there is a series of binding sites (S) that favour particular amino acids (P). This level of specificity ensures that proteases carry out their task only when truly needed.

Primary information retrieved from public and private sequencing projects, combined with data from the Merops, InterPro, and Ensembl databases, total of 553 genes have been annotated that encode proteases or protease homologues in the human genome. Mouse genome contains 628 proteases and protease homologues.

                                               Table: The human and mouse protease genes and pseudogenes.

References:

Lander, E.S., Linton, L.M., Birren, B., Nusbaum, C., et al., 2001. Initial sequencing and analysis of the human genome. Nature. 409(6822), 860-921.

Pietzsch, J., 2003. Signalling scissors: New perspectives on proteases. Horizon Symposia.

Puente, X.S., Sánchez, L.M., Overall, C.M., López-Otín, C., 2003. Human and mouse proteases: a comparative genomic approach. Nat Rev Genet. 4(7), 544-558.

Venter, J.C., Adams, M.D., Myers, E.W., Li, P.W., et al., 2001. The sequence of the human genome. Science. 291(5507), 1304-1351. 

Copyright © 2017 HS Counseling. All rights reserved. 

Shape your future by subsidising brain

Majority of the population invest in house, car, share market etc., believing that the investment they are doing is for the betterment of their future. But little do they know that these investments are fluctuating and are only the superficial ones.  It is like an exterior bubble which can be burst by mere crash of the property rates and stock market.  The most profitable investment one can ever make is investing in your brain.

Talking about the money, investment, future and brain, I have recollected one paraphrase, “Don’t run behind success and money, try to achieve excellence by sharpening your brain, knowledge and skills, success and money will automatically come looking for you”.

Truer words have never been spoken.

Brain is a very important organ in the human body as it allows a person to think, visualize, feel and store memories. Thinking and creative visualization are the key to success. Being more proficient will make you imperative in every area of your life. Inflation or recession, irrespective of the economy scenario, nurtured mind will always yield valuable returns.  The assured way to achieve a quality and successful life is to invest wisely in brain.

Learning new things, reading a lot, communicating with people from different backgrounds, participating in group discussions and playing educational games are some of the ways to foster your mental ability. These simple ways might help in brain development and function but might not be good enough to excel the brain activity. Here nootropics may be able to fill the gap. 

Nootropics are the drugs that help improve the mental functions.  These drugs hold the promise of helping with memory, cognitive ability, concentration, decision making, thinking and problem solving. These supplements are considered to work by amending availability of the brain’s supply of neurotransmitters, hormones and enzymes with escalated oxygen. Various nootropic drugs are available in the form of supplements. Apex GPA is a natural supplement and is even certified by Health Canada. If consumed as per the recommendation, it significantly improves memory, alertness and intellectual performances.

Investing in your mind truly shapes your future. It allows you to be skillful, proficient and compelling person.

Source: https://www.apexgpa.com/shape-future-subsidising-brain/

Smart drugs to revitalize intellectual power

In today’s competitive world, it won’t be wrong to say that ‘life is a race and everybody is contesting to win’. Three quintessential elements have been prominently reported to help gain an edge over the others which are:

-Having a good memory

-Being insightful

-Thinking on the feet

They sound too simple but aren’t naturally so commonplace. You must’ve found yourself in situations where you have two papers to write in a day and have completed its preparation 15 days in advance thinking that a short revision would do the trick. However, just the evening before…uh-oh… difficult to recall what you studied…unable to think new…lack of vision… Isn’t it?

How about getting smarter just by tossing a pill? It sounds too good to be true like in a TV commercial where you apply a muscle relief spray and get back on the soccer field in another 15 minutes. But ‘Smart drugs’ do exist and top notch researchers, globally, have proved the improvement in mental abilities on the ingestion of such drugs. Cognitive enhancers and Nootropics are the other names for Smart drugs.  

Smart drugs are the drugs that work on the human brain to improve memory, learning, attention, perception, reasoning, organization, social skills and vision. These drugs are often linked with neurological or mental disorders, but research evidence shows that regular people can get smarter by swallowing these drugs. Brain function and cognition is preserved by these drugs and hence, they serve as neuroprotective agents.

Various smart drugs are available in the form of supplements. Mechanism of action differs from one drug to the other and is very significant to consider. Age, dosage, duration, frequency and lifestyle are some of the key factors that should be taken into consideration before resorting to any drug. Any kind of negligence may alter the drug from being benignant to malignant.

Apex GPA supplements are composed of natural ingredients and are even certified by Health Canada. Scientific literature has reported that ingredients viz. Caffeine, Panax Ginseng and Ginkgo Biloba significantly improve calmness, alertness, concentration, attention, memory, accuracy and physical performance. If ingested as per the recommendation, you will never lag behind in terms of memory, concentration and alertness.

The underlying message is that the Smart drugs are innocuously beneficial if used with care.  

Source: https://www.apexgpa.com/smart-drugs-to-revitalize-intellectual-power/

Antibody purification

Buffers and Reagents:

Column: HiTrap NHS-activated HP 1 ml

Coupling buffer - 0.2 M NaHCO₃ , 0.5 M NaCl, pH 8.3

Buffer A - 0.5 M Ethanolamine, 0.5 M NaCl, pH 8.3

Buffer B - 0.1 M Sodiumacetate, 0.5 M NaCl, pH 4.0

1 mM HCl

2 M glycine-HCl pH 2.0

0.1% PBS/NaN₃

PBS

50 mM glycine-HCl pH 2.75

50 mM TAE pH 11.5

Buffer A - 0.5 M Ethanolamine, 0.5 M NaCl, pH 8.3

Buffer B - 0.1 M Sodiumacetate, 0.5 M NaCl, pH 4.0

Protocol:

Preparation of the peptide: Weigh 5 mg of the peptide and dissolve in 1 ml coupling buffer by vortexing.

Determine the protein concentration by measuring absorption at 280 nm using spectrophotometer.

Coupling to the column-

Fill 5 ml syringe with 1 mM HCl. Couple the column by placing the syringe on the yoke of the column.

Activation of the column-

Activate the column and wash away the isopropanol from the column by passing 6 ml of 1 mM HCl through the column. 

Coupling of the peptide-

Connect the column with two syringes, one on the upper side and other on the lower side. Fill the upper syringe with peptide solution and press it slowly on the column. The upper syringe will be empty and lower will be filled up half. Incubate the column for 1 hour at 4 ^oC. Then press the lower syringe slowly in order to move the solution to the upper syringe. Again incubate the set up at 4 ^oC for 1 hour. Move the peptide solution once every hour between two syringes for up to 4 hours. Incubate the whole set up at 4 ^oC overnight. 

Next day-

Remove the lower syringe and let the peptide solution drop out of the column. Preserve the flow through.

Washing of the column-

Wash the column twice using 1 ml coupling buffer. Preserve the flow through and mix it with the previous one. Mix 1 ml of the flow through with 1 ml of 2 M glycine-HCl pH 2.0 and measure the absorption at 280 nm. 

Determination of the coupling efficiency-

Volume of the coupled peptide solution:

A = A_{280, coupling solution} X V_{loaded volume of coupling solution}

Volume of the not coupled peptide:

B = A_{280, post-coupling wash after acidification} X V_{Volume post-column wash} X 2_{(dilution when acidified)}

Coupling yield, %:

(A-B)/A x 100 = Z

Z% of the peptide solution is coupled to the column. 

Denaturation of the column-

Denature the column by passing 2 ml of buffer A, 2 ml of buffer B and again 2 ml of buffer A. Repeat the sequence thrice and incubate the column at 25 ^oC for 30 minutes. Post 30 minutes, pass 2 ml of buffer B, 2 ml of buffer A and 2 ml of buffer B through the column and repeat the sequence thrice followed by incubation at 25 ^oC for 30 minutes.

Equilibration of the column-

Equilibrate the column by washing it with 10 ml of PBS once. 

Storage of the column-

Add 2 ml of 0.1% PBS/NaN₃ to the column and store the column at 4 ^oC.

Antibody purification-

1. Defrost the bleed and take 10 ml out. Freeze back the rest of the bleed at -80 ^oC.

2. Centrifuge the serum at 40,000 rpm, for 1 hour at 4 ^oC using ultracentrifuge.

L1 = clear, thick layer

L2 = pink, thin layer

3. Remove the L2 layer carefully with pasteur pipette and place it on ice.

4. Wash the coupled column with 10 ml of PBS.

5. Absorb the serum in a 5 ml syringe and place it on the column. Arrange the second syringe at the other end of the column.

6. Move the serum within the syringes every 15 minutes for up to 3 hours at 4 ^oC.

7. Collect the sample from the flow through.

8. Wash the column using 10 ml of PBS.

9. Elute the antibody with 10 ml of 50 mM glycine-HCl pH 2.75 and place the eluate on ice.

10. Again wash the column using 10 ml of PBS.

11. Elute the antibody with 10 ml of 50 mM TAE pH 11.5 and place the eluate on ice.

12. Wash the column using 20 ml of PBS and store the column in PBS/NaN₃ at 4 ^oC.

13. Concentrate the eluates to a volume of 4 ml using 30 kDa Amicon’s membranes. Thereafter, dialyse the eluates in PBS for 2 hours and then in PBS/50% Glycerol overnight at 4 ^oC.