Modifications in the muscle acylphosphatase purification procedure enabled us to isolate the enzyme with its sole cysteine in the -SH form; this enzyme form is the most abundant in vivo. Our data demonstrates that the enzyme forms purified by previously reported procedures can be easily derived from a reaction of the SH-enzyme with oxidized glutathione. Probably most, or even all, of these enzyme forms are artifacts due to the purification. The SH-acylphosphatase shows kinetic parameters similar to those reported for the mixed disulfide with glutathione and S-S dimer, except for the specific activity value, which is about twice as much, and the Km, which is reduced.

Purification and characterization of rabbit muscle acylphosphatase in the thiol (-SH) form / A. Berti; M. Stefani; G. Camici; G. Manao; G. Cappugi; D. Degl'Innocenti; G. Ramponi. - In: INTERNATIONAL JOURNAL OF PEPTIDE & PROTEIN RESEARCH. - ISSN 0367-8377. - STAMPA. - 28:(1986), pp. 15-21.

Purification and characterization of rabbit muscle acylphosphatase in the thiol (-SH) form.

BERTI, ANDREA;STEFANI, MASSIMO;CAMICI, GUIDO;MANAO, GIAMPAOLO;CAPPUGI, GIANNI;DEGL'INNOCENTI, DONATELLA;RAMPONI, GIAMPIETRO
1986

Abstract

Modifications in the muscle acylphosphatase purification procedure enabled us to isolate the enzyme with its sole cysteine in the -SH form; this enzyme form is the most abundant in vivo. Our data demonstrates that the enzyme forms purified by previously reported procedures can be easily derived from a reaction of the SH-enzyme with oxidized glutathione. Probably most, or even all, of these enzyme forms are artifacts due to the purification. The SH-acylphosphatase shows kinetic parameters similar to those reported for the mixed disulfide with glutathione and S-S dimer, except for the specific activity value, which is about twice as much, and the Km, which is reduced.
1986
28
15
21
A. Berti; M. Stefani; G. Camici; G. Manao; G. Cappugi; D. Degl'Innocenti; G. Ramponi
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/323512
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