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PMID: 7236200 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

A comparison of potato and vertebrate lactate dehydrogenases.

The Biochemical journal ·Vol. 191 ·No. 2 ·1980-11-01 ·Pages 341-8

Poerio E, Davies DD

Abstract

A 2000-fold purification of L(+)-lactate dehydrogenase from potatoes is reported. Five isoenzymes of lactate dehydrogenase can be detected in crude extracts of potato, and three of these are present in the purified preparation. The enzyme (mol.wt. 150 000), which is composed of four subunits (mol.wt. 37 500), is active with the same oxo acids and hydroxy acids that have been reported as substrates with the same oxo acids and hydroxy acids that have been reported as substrates for vertebrate lactate dehydrogenases. These similarities between potato and vertebrate lactate dehydrogenases contrast sharply with some other reports on potato lactate dehydrogenase. These discrepancies are discussed in relation to the proposition that vertebrate and potato lactate dehydrogenases share a common evolutionary origin.

MeSH Terms
Adenosine Triphosphate/pharmacology Chemical Phenomena Chemistry Isoenzymes Kinetics L-Lactate Dehydrogenase/antagonists & inhibitors,isolation & purification Oxalates/pharmacology Oxamic Acid/pharmacology Plants/enzymology Substrate Specificity
Chemicals
Isoenzymes Oxalates Adenosine Triphosphate L-Lactate Dehydrogenase Oxamic Acid
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Poerio E
Davies D D
References (16)
16 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1980-11-01
Pages
341-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1162223
Subset
IM
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