Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms

摘要: Abstract Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This considerably milder than the preceding one, gave overall yield of about 60% activity permitted isolation three molecular forms with acylphosphatase activity. All these enzymatic are tightly bound to Sepharose 4B-linked anti-horse antibodies. Two (Ho1 Ho3) present in larger amounts: Ho1 corresponds enzyme according older procedure; this is mixed disulfide between main chain 98 amino acid residues glutathione. Ho2 differs only chemical nature molecule(s) SS sole cysteine at position 21 chain. Ho3 dimer polypeptide Ho1, Ho2, elicit very similar kinetic parameters presence benzoylphosphate as substrate.