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- W2024456438 abstract "The complexation of bovine trypsin with potassium poly(vinyl alcohol sulphate) (KPVS) was investigated at different pHs by means of colloid titration. The number of moles of the basic (amino, imidazolyl, and guanidyl) groups in 1 g of trypsin, which were bound to the sulphate groups in KPVS by salt linkages, was evaluated from the titration data. From a comparison of the results obtained with the number of basic groups counted from the amino acid sequence already reported, it was found that the complexation follows a stoichiometric relationship in the range pH <3 where all the basic groups in trypsin are protonated. The enzymatic activity of the resulting stoichiometric complex was examined by using Nα-benzoyl-dl-arginine-p-nitroanilide and casein as substrates. The complexed enzyme showed appreciable retention of activity, not only towards the low molecular weight substrate but also towards the polymeric substrate. Therefore, it became apparent that the stoichiometric complexation of trypsin with KPVS does not have a large influence on conditions for the active site of the enzyme, because the salt linkages for maintaining the structure of the complex are very loose." @default.
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- W2024456438 title "Stoichiometric complexation of bovine trypsin with potassium poly(vinyl alcohol sulphate) and enzymatic activity of the complex" @default.
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