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A pepsinogen from rainbow trout. Comp Biochem Physiol B 1983;75(1):109-12

Date

01/01/1983

Pubmed ID

6406134

DOI

10.1016/0305-0491(83)90046-9

Scopus ID

2-s2.0-0020654759 (requires institutional sign-in at Scopus site)   49 Citations

Abstract

1. A pepsinogen, Ia on the basis of its electrophoretic mobility, from rainbow trout stomach, has an optimum pH near 2 for activation. 2. The cognate pepsin is denatured at pH values above 7, in contrast to the zymogen, which is slightly more alkali-stable. It has an optimum pH of 3 for proteolysis of denatured hemoglobin. 3. The intrinsic reactivity of the zymogen and pepsin (rates of activation and of proteolysis, respectively) are quite high, but as they operate at the environmental temperature of the fish, are remarkably similar to rates of activation and proteolysis by mammalian pepsinogens and pepsins.

Author List

Twining SS, Alexander PA, Huibregtse K, Glick DM

Author

Sally S. Twining PhD Assistant Dean, Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Drug Stability
Enzyme Activation
Hydrogen-Ion Concentration
Pepsin A
Pepsinogens
Salmonidae
Stomach
Thermodynamics
Trout