Immobilized hybrids of glyceraldehyde-3-phosphate dehydrogenase.
Biochim Biophys Acta, 1978/7/07;525(1):291-4.
Muronetz VI, Asryants RA, Nagradova NK
PMID: 28768
Abstract
Yeast glyceraldehyde-3-phosphate dehydrogenase (glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12) immobilized on CNBr-activated Sepharose 4-B has been subjected to dissociation to obtain matrix-bound dimeric species of the enzyme. Hybridization was then performed using soluble glyceraldehyde-3-phosphate dehydrogenase isolated from rat skeletal muscle. Immobilized hybrid tetramers thus obtained were demonstrated to exhibit two distinct pH-optima of activity characteristic of the yeast and muscle enzymes, respectively. The results indicate that under appropriate conditions the activity of each of the dimers composing the immobilized hybrid tetramer can be studied separately.
MeSH terms
Animals; Enzymes, Immobilized; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrogen-Ion Concentration; Macromolecular Substances; Muscles; Protein Multimerization; Rats; Saccharomyces cerevisiae
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