Reconstitution of the electrophoretic complexity of mouse lactate dehydrogenase

Dudman N.P.B. (1969) Reconstitution of the electrophoretic complexity of mouse lactate dehydrogenase. Biochemical and Biophysical Research Communications, 36 4: 608-613. doi:10.1016/0006-291X(69)90348-9

Author Dudman N.P.B.
Title Reconstitution of the electrophoretic complexity of mouse lactate dehydrogenase
Journal name Biochemical and Biophysical Research Communications   Check publisher's open access policy
ISSN 0006-291X
Publication date 1969-08-15
Sub-type Article (original research)
DOI 10.1016/0006-291X(69)90348-9
Open Access Status Not yet assessed
Volume 36
Issue 4
Start page 608
End page 613
Total pages 6
Language eng
Subject 1312 Molecular Biology
1304 Biophysics
1303 Specialist Studies in Education
Abstract The residues which are covalently joined by disulphide bonds to mouse lactate dehydrogenase, and which affect the electrophoretic behaviour of the enzyme, have been isolated and identified as cysteine and glutathione. Oxidation of partially purified and previously reduced mouse muscle lactate dehydrogenase, in a solution containing a mixture of cysteine and glutathione, results in an electrophoretic pattern of the enzyme apparently identical with that of the native enzyme. The possibility that the polypeptide subunits of lactate dehydrogenase may exert a selective effect in their reactions with cysteine and reduced glutathione is discussed, and the likelihood that complex electrophoretic patterns of enzymes other than mouse lactate dehydrogenase may be caused by covalently bound simple metabolites is noted.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
Version Filter Type
Citation counts: Scopus Citation Count Cited 8 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 14 Jun 2016, 14:13:24 EST by System User