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- W2057934582 abstract "1 A protease, purified from the growth medium of Acremonium kiliense Grütz, has a pH optimum of 10.5 for the hydrolysis of casein. 2 It hydrolyzes the reduced, carboxymethylated B-chain of bovine insulin at 13 points, principally those next to the carboxyl group of aromatic and hydrophobic amino acids, but not at the basic amino acid residues. 3 It does not hydrolyze dipeptides, benzoyl arginine ethyl ester or glutaryl-l-phenylalanine-p-nitroanilide. 4 The enzyme can be titrated with N-trans-cinnamoyl imidazole and assayed with the p-nitrophenyl esters of benzoyloxycarbonyl amino acids. 5 The enzymic hydrolysis of N-acetyl phenylalanine ethyl ester can be followed by an absorbance change at 221 nm or by means of a pH-stat. Analysis of the variation of Km and V with pH for this substrate suggests that there is a group involved in the activity which has a pK of 6.6 in the free enzyme and in the active enzyme · substrate complex. 6 It is inhibited by diisopropylphosphofluoridate and phenylmethylsulphonyl fluoride, suggesting that it is a serine protease. It is unaffected by metals, metal-chelating agents, iodoacetate or 2-mercaptoethanol." @default.
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- W2057934582 date "1972-07-01" @default.
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- W2057934582 title "An Alkaline Protease from Acremonium kiliense. Specificity, Kinetics, and Effect of pH" @default.
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- W2057934582 doi "https://doi.org/10.1111/j.1432-1033.1972.tb01929.x" @default.
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