Báo cáo khoa học: Detection of native peptides as potent inhibitors of enzymes Crystal structure of the complex formed between treated bovine a-chymotrypsin and an autocatalytically produced fragment, Ile-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp, at 2.2 A˚ resolution
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Chymotrypsin is a prominent member of the family of serine proteases. The present studies demonstrate the presence of a native fragment contain-ing 14 residues from Ile16 to Trp29 in a-chymotrypsin that binds to chy-motrypsin at the active site with an exceptionally high affinity of 2.7 ± 0.3·10 )11 mand thus works as a highly potent competitive inhib-itor. The commercially available a-chymotrypsin was processed through a three phase partitioning system (TPP). The treated enzyme showed consid-erably enhanced activity. ...
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