Publication Date:
1980-02-15
Description:
Isozymes of lactate dehydrogenase from heart and muscle of Atlantic hagfish show less functional divergence than those from other fishes and higher vertebrates. The enzyme from hagfish heart (B4) displays a higher Michaelis constant for pyruvate and lower substrate inhibition at moderate pyruvate concentrations than heart isozymes from other species. These properties support the hypothesis that the ancestral vertebrate lactate dehydrogenase was a muscle (A4)-type enzyme and also suggest a role for the B4 enzyme in the unusual physiology of hagfish cardiac tissue which functions under sustained hypoxic conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidell, B D -- Beland, K F -- New York, N.Y. -- Science. 1980 Feb 15;207(4432):769-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352286" target="_blank"〉PubMed〈/a〉
Keywords:
Anaerobiosis
;
Animals
;
*Biological Evolution
;
Energy Metabolism
;
Fishes/genetics/*physiology
;
Genes
;
Isoenzymes
;
Kinetics
;
L-Lactate Dehydrogenase/*genetics/metabolism
;
Muscles/*enzymology
;
Myocardium/enzymology
;
Pyruvates/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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