Nonreversibility in the Reductive Denaturation of Chymotrypsinogen A

Autor:	Brown Jc, Horton Hr
Rok vydání:	1972
Předmět:	chemistry.chemical_classification Chromatography Chymotrypsin biology Chemistry Chymotrypsinogen Polypeptide chain Trypsin General Biochemistry Genetics and Molecular Biology CHYMOTRYPSINOGEN A Enzyme Biochemistry biology.protein medicine Denaturation (biochemistry) Chemical stability medicine.drug
Zdroj:	Experimental Biology and Medicine. 140:1451-1455
ISSN:	1535-3699 1535-3702
DOI:	10.3181/00379727-140-36694
Popis:	SummaryInvestigation of the air-reoxidation of denatured, fully reduced chymotrypsinogen A resulted in a maximum recovery of 1.4% of enzymatically active chymotrypsin upon treatment with trypsin. Under the same conditions, urea-denatured chymotrypsinogen, which had not been reduced, yielded 100% recovery of enzymatic activity. Thus the biologically functional conformation of the polypeptide chain comprising chymotrypsinogen may not be that of greatest thermodynamic stability.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::504acaf0b61231b2a654c3fd4de6f793 https://doi.org/10.3181/00379727-140-36694 Zobrazit plný text záznamu