ON THE MECHANISM OF ENZYME ACTION. LXX. UREA DENATURATION OF TRYPSIN AND ACYLTRYPSINS
Journal Article
·
· Archives of Biochemistry and Biophysics (U.S.)
Trypsin and its acetyl and succinyl derivatives were exposed to urea solutions of various concentrations. The resulting changes, as measured by activity and sedimentation studies, are due to denaturation, both reversible and irreversible, and to self-digestion. The effect of acylation on these processes is discussed, and in addition the sequence of steps leading to the final inactive product is considered. The action of urea is compared to that of heating the enzymes, and the similarities are indicated. (auth)
- Research Organization:
- Fordham Univ., New York
- Sponsoring Organization:
- USDOE
- NSA Number:
- NSA-14-022738
- OSTI ID:
- 4156381
- Journal Information:
- Archives of Biochemistry and Biophysics (U.S.), Journal Name: Archives of Biochemistry and Biophysics (U.S.) Vol. Vol: 90; ISSN ABBIA
- Country of Publication:
- Country unknown/Code not available
- Language:
- English
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