An erythrocyte isoenzyme of acylphosphatase was purified from bovine red cells. The protein was characterized as regards the kinetic parameters and amino acid sequence. A simple and rapid sequencing strategy, based on a few experiments, was used for reconstructing the primary structure of the enzyme, since the purification procedure gave a very low yield. The length of the polypeptide chain is 100 residues. Comparison with the analogous human isoenzyme indicates that the primary structure is about 90% conserved. The presence of two additional residues at the acetylated N-terminus confirms the hypervariability for this region found in other acylphosphatases.

Purification, kinetic properties and primary structure of bovine erythrocyte acylphosphatase / L. Pazzagli; U. Ikram; G. Liguri; N. Taddei; A. Gentilini; C. Cecchi; G. Manao; G. Cappugi;. - In: ITALIAN JOURNAL OF BIOCHEMISTRY. - ISSN 0021-2938. - STAMPA. - 42:(1993), pp. 233-245.

Purification, kinetic properties and primary structure of bovine erythrocyte acylphosphatase

PAZZAGLI, LUIGIA;LIGURI, GIANFRANCO;TADDEI, NICCOLO';GENTILINI, ALESSANDRA;CECCHI, CRISTINA;MANAO, GIAMPAOLO;CAPPUGI, GIANNI
1993

Abstract

An erythrocyte isoenzyme of acylphosphatase was purified from bovine red cells. The protein was characterized as regards the kinetic parameters and amino acid sequence. A simple and rapid sequencing strategy, based on a few experiments, was used for reconstructing the primary structure of the enzyme, since the purification procedure gave a very low yield. The length of the polypeptide chain is 100 residues. Comparison with the analogous human isoenzyme indicates that the primary structure is about 90% conserved. The presence of two additional residues at the acetylated N-terminus confirms the hypervariability for this region found in other acylphosphatases.
1993
42
233
245
L. Pazzagli; U. Ikram; G. Liguri; N. Taddei; A. Gentilini; C. Cecchi; G. Manao; G. Cappugi;
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/321847
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