Affordable Access

Publisher Website

Lactate dehydrogenase function inElectrophorusswimbladder and in the lungfish lung

Authors
Journal
Comparative Biochemistry and Physiology
0010-406X
Publisher
Elsevier
Publication Date
Volume
27
Issue
2
Identifiers
DOI: 10.1016/0010-406x(68)90260-0

Abstract

Abstract 1. 1. Lactate dehydrogenase (LDH) affinity for pyruvate is twofold to threefold higher at pH 6·0 than at pH7·9 in the case of swimbladder and lung LDHs. 2. 2. For the swimbladder LDH, but not the lung LDH, optimal velocity and substrate inhibition are higher at pH 6·0 than at pH 7·9. 3. 3. These effects of pH appear to be adaptive.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Lactate dehydrogenase function in Electrophorus sw...

on Comparative biochemistry and p... November 1968

The nature of the thermal optimum for lungfish lac...

on Comparative Biochemistry and P... Jan 01, 1968

The nature of the thermal optimum for lungfish lac...

on Comparative biochemistry and p... November 1968

Save the lungfish.

on Nature Jul 20, 2006
More articles like this..