Immobilized subunits can function as an affinity sorbent to purify oligomeric enzymes: the usefulness of hybridization on the solid support.
Immobilized dimers of yeast glyceraldehyde-3-phosphate dehydrogenase covalently bound to sepharose were shown to form hybrids with soluble dimers of the homologous enzymes present in crude tissue extracts (rats skeletal muscle, rat, rabbit and bovine hearts, rat liver, rat brain). Immobilized hybrid tetramers were then dissociated to form purified soluble enzymes.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002417:Cattle; D002846:Chromatography, Affinity / Q000379:methods; D004800:Enzymes, Immobilized; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D055503:Protein Multimerization; D011817:Rabbits; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D004800:Enzymes, Immobilized; D046911:Macromolecular Substances; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases