Effect of anions on the structure of glyceraldehyde-3-phosphate dehydrogenase from rat skeletal muscle

Glyceraldehyde-3-phosphate dehydrogenase from rat skeletal muscle undergoes reversible partial dissociation into 4.2–4.5 S fragments at +4°C and at protein concentrations as high as 8–9 mg/ml, depending upon the anion species present. The order of effectiveness of various anions in dissociating acti...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 43; no. 4; pp. 840 - 846
Main Authors Nagradova, N.K., Guseva, M.K.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 21.05.1971
Subjects
Acetates
Animals
Bromides
Chemical Phenomena
Chemistry
Chlorides
Citrates
Dialysis
Drug Stability
Glyceraldehyde-3-Phosphate Dehydrogenases - antagonists & inhibitors
Ions
Muscles - enzymology
Nitrates
Phosphates
Potassium
Potassium Chloride
Potassium Iodide
Quaternary Ammonium Compounds
Rats
Sodium
Sodium Chloride
Sulfates
Temperature
Ultracentrifugation
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Summary:Glyceraldehyde-3-phosphate dehydrogenase from rat skeletal muscle undergoes reversible partial dissociation into 4.2–4.5 S fragments at +4°C and at protein concentrations as high as 8–9 mg/ml, depending upon the anion species present. The order of effectiveness of various anions in dissociating activity corresponds to their position in the Hofmeister series: bromide > nitrate > chloride > acetate > sulfate > phosphate=citrate. Quite similar is the order of activity of anions in their influence on the thermal stability of the dehydrogenase.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(71)90693-0