Purification and properties of enolase from carp ( Cyprinus carpio). Comparison with enolases from mammals' muscles and yeast

1. 1. The enolase (2-phospho- d-glycerate hydrolyase E.C. 4.2.1.11) from carp muscle was obtained, the specific activity—88 U/mg of protein. 2. 2. K m for 2-phosphoglycerate was 0.313 mM and for phosphoenolpyruvate—0.76 mM. 3. 3. The enzyme is active only in the presence of divalent metal ions, Mg 2...

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Published inComparative biochemistry and physiology. B, Comparative biochemistry Vol. 75; no. 4; pp. 693 - 698
Main Authors Pietkiewicz, Jadwiga, Kustrzeba-Wójcicka, Irena, Wolna, Elżbieta
Format Journal Article
LanguageEnglish
Published England Elsevier Inc 1983
Subjects
animal physiology
Animals
aquatic organisms
Carps - metabolism
Cyprinidae - metabolism
Cyprinus carpio
enzymatic activity
Freshwater
Humans
Kinetics
Mammalia
Molecular Weight
muscles
Muscles - enzymology
Phosphates - pharmacology
Phosphopyruvate Hydratase - isolation & purification
physicochemical properties
Saccharomyces cerevisiae - enzymology
Species Specificity
Swine
yeasts
EDTA
β-ME
Tris
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Summary:1. 1. The enolase (2-phospho- d-glycerate hydrolyase E.C. 4.2.1.11) from carp muscle was obtained, the specific activity—88 U/mg of protein. 2. 2. K m for 2-phosphoglycerate was 0.313 mM and for phosphoenolpyruvate—0.76 mM. 3. 3. The enzyme is active only in the presence of divalent metal ions, Mg 2+ being the best activator. 4. 4. The phosphate and fluoride decreased the activity of enzyme. 5. 5. The molecular weight of the dimeric form of enzyme was found to be 93,000. 6. 6. The enzyme is immunologically different from pig muscle enolase.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0305-0491
DOI:10.1016/0305-0491(83)90118-9