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

Affinity chromatographic purification of horse muscle acylphosphatase: evidence of the existence of multiple molecular forms / G. MANAO ; G. CAMICI ; M. STEFANI ; A. BERTI ; G. CAPPUGI; G. LIGURI ; P. NASSI ; G. RAMPONI. - In: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS. - ISSN 0003-9861. - STAMPA. - 226(2):(1983), pp. 414-424.

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

MANAO, GIAMPAOLO;CAMICI, GUIDO;STEFANI, MASSIMO;BERTI, ANDREA;CAPPUGI, GIANNI;LIGURI, GIANFRANCO;NASSI, PAOLO ANTONIO;RAMPONI, GIAMPIETRO
1983

Abstract

Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) S-S bound to the sole cysteine present at position 21 of the main chain. Ho3 is an S-S dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate.
1983
226(2)
414
424
G. MANAO ; G. CAMICI ; M. STEFANI ; A. BERTI ; G. CAPPUGI; G. LIGURI ; P. NASSI ; G. RAMPONI
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/308906
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