A pepsinogen from rainbow trout. Comp Biochem Physiol B 1983;75(1):109-12
Date
01/01/1983Pubmed ID
6406134DOI
10.1016/0305-0491(83)90046-9Scopus ID
2-s2.0-0020654759 (requires institutional sign-in at Scopus site) 49 CitationsAbstract
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 DMAuthor
Sally S. Twining PhD Assistant Dean, Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsDrug Stability
Enzyme Activation
Hydrogen-Ion Concentration
Pepsin A
Pepsinogens
Salmonidae
Stomach
Thermodynamics
Trout