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- W2526442236 abstract "Calcineurin is a calcium dependent protein ser/thr phosphatase. The assay of this enzyme has been done by using various substrates since it has shown promising evidences to act upon para-nitrophenylphosphate (p-'PP) and many phosphopeptide analogues as well. But none of the methods are as reliable as far sensitivity of the method is concerned. To address the assay method for the Calcineurin, we have isolated and partially purified the enzyme from the bovine brain and employed substrate like p-'PP with two different metal ions (Calcium and Manganese). We have established the binding affinity studies by using enzyme kinetics. The binding affinity of p-'PP against particular metal ion shows the better metal activator and substrate for the enzyme. The affinity in presence of calcium for the substrates p-'PP is found to be Km= 0.48 mM. The affinity in presence of manganese for the substrates p-'PP, is found to be Km= 0.77 mM. At the same time we have used Autodock 3.05 for minimal binding energy calculations for the p-'PP, the 1st cluster which had the maximum number of runs (30) reported mean dock energy of -4.24 kcal / mol. We conclude from the study that p-'PP has more affinity toward the calcineurin in presence of Calcium than Manganese. Copyright© (2010) by the International Society for Research in Science and Technology." @default.
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- W2526442236 date "2010-01-01" @default.
- W2526442236 modified "2023-09-27" @default.
- W2526442236 title "In silico and pharmacokinetics of para-nitrophenylphosphate substrate for calcineurin" @default.
- W2526442236 hasPublicationYear "2010" @default.
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