Lactate Dehydrogenase Isoenzymes in Chicken Tissues

LACTATE dehydrogenase isoenzymes from a variety of animal sources have been reported to differ in a number of their properties, including substrate affinities 1,2 , utilization of coenzyme analogues 3 , substrate specificity 4 , thermal stability 5 and sensitivity to inhibitors 6,7 . A regular grada...

Full description

Saved in:
Bibliographic Details
Published in:Nature (London) 1967-02, Vol.213 (5075), p.513-514
Main Author: WITHYCOMBE, WENDY A
Format: Article
Language:English
Subjects:
Animals
Birds
Butyrates
Electrophoresis
Female
Humanities and Social Sciences
Humans
Isoenzymes
L-Lactate Dehydrogenase - analysis
letter
Male
multidisciplinary
Muscles - enzymology
Myocardium - enzymology
Pyruvates
Science
Science (multidisciplinary)
Spectrophotometry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:LACTATE dehydrogenase isoenzymes from a variety of animal sources have been reported to differ in a number of their properties, including substrate affinities 1,2 , utilization of coenzyme analogues 3 , substrate specificity 4 , thermal stability 5 and sensitivity to inhibitors 6,7 . A regular gradation in these properties has been found which appears to correlate with the difference in electrophoretic mobility of each isoenzyme fraction. This difference is thought 8,9 to be determined by their A and B sub-unit composition. According to these workers,. LD 1 and LD 5 are “pure types” comprising four B and four A sub-units, respectively, and LD 2–4 are intermediate hybrid types. Cahn et al. 9 report the presence of five lactate dehydrogenase isoenzymes in young chicken tissues, the heart muscle isoenzyme being a tetramer of four B sub-units and the breast muscle isoenzyme a tetramer of four A sub-units. We could not confirm the existence of five bands of activity in adult tissues, and this communication reports studies on isoenzymes derived from adult chicken tissues which showed different properties but similar electrophoretic mobility.
ISSN:0028-0836
1476-4687
DOI:10.1038/213513a0