An acylphosphatase has been purified from turkey muscle in a rapid and high-yield way. The enzyme has been characterized for structural, kinetic, and immunological parameters, as well as with regard to its stability to thermal, urea, and phenylglyoxal inactivation. The enzyme is quite different from the turkey muscular isoenzyme, and shows structural and kinetic properties that are very similar to those previously reported for the erythrocyte isoenzyme from human erythrocytes and from chicken muscle. From the data reported it appears that this enzyme corresponds to the acylphosphatase erythrocyte isoenzyme. Unlike the erythrocyte isoenzymes studied so far, this enzyme is able to cross-react with antibodies that are

Purification and characterization of acylphospatase erythrocyte isoenzyme from turkey muscle / M. STEFANI ; D. DEGL'INNOCENTI ;A. BERTI ; G. CAPPUGI; G. MANAO ; G. CAMICI ; G. RAMPONI. - In: JOURNAL OF PROTEIN CHEMISTRY. - ISSN 0277-8033. - STAMPA. - 9:(1990), pp. 633-640.

Purification and characterization of acylphospatase erythrocyte isoenzyme from turkey muscle

STEFANI, MASSIMO;DEGL'INNOCENTI, DONATELLA;BERTI, ANDREA;CAPPUGI, GIANNI;MANAO, GIAMPAOLO;CAMICI, GUIDO;RAMPONI, GIAMPIETRO
1990

Abstract

An acylphosphatase has been purified from turkey muscle in a rapid and high-yield way. The enzyme has been characterized for structural, kinetic, and immunological parameters, as well as with regard to its stability to thermal, urea, and phenylglyoxal inactivation. The enzyme is quite different from the turkey muscular isoenzyme, and shows structural and kinetic properties that are very similar to those previously reported for the erythrocyte isoenzyme from human erythrocytes and from chicken muscle. From the data reported it appears that this enzyme corresponds to the acylphosphatase erythrocyte isoenzyme. Unlike the erythrocyte isoenzymes studied so far, this enzyme is able to cross-react with antibodies that are
1990
9
633
640
M. STEFANI ; D. DEGL'INNOCENTI ;A. BERTI ; G. CAPPUGI; G. MANAO ; G. CAMICI ; G. RAMPONI
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/205318
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