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Purification and characterization of acylphosphatase erythrocyte isoenzyme from turkey muscle.

作者信息

Stefani M, Degl'Innocenti D, Berti A, Cappugi G, Manao G, Camici G, Ramponi G

机构信息

Department of Biochemical Sciences, University of Florence, Italy.

出版信息

J Protein Chem. 1990 Oct;9(5):633-40. doi: 10.1007/BF01025017.

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 raised against the muscular isoenzyme.

摘要

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