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The low molecular weight acid phosphatase ec 3.1.3.2 from bovine liver isolation amino acid composition and chemical modification studies


Archives of Biochemistry and Biophysics 206(1): 122-131
The low molecular weight acid phosphatase ec 3.1.3.2 from bovine liver isolation amino acid composition and chemical modification studies
The smallest of the 3 MW forms of acid phosphatase from bovine liver was purified to a specific activity of 100 .mu.mol min-1 mg-1 (measured at pH 5.5 and 37.degree. C with p-nitrophenyl phosphate). Using several chromatographic and electrophoretic methods, no evidence of heterogeneity was detected. The enzyme was characterized with respect to its stability as a function of pH, MW, amino acid composition, steady-state kinetic parameters in the pH range 4-7 and inhibition by common acid phosphate inhibitors at pH 5.5. The amino acid composition differed from a previous literature report. The enzyme was stoichiometrically inactivated upon incubation with Hg2+, Ag+ and iodoacetate. Inactivation occurred upon photoinactivation in the presence of Rose Bengal, but no inactivation occurred with diethyl pyrocarbonate. The alkylation of one of 5 cysteine residues by iodoacetate caused complete inactivation of the enzyme. This alkylation was prevented by the presence of phosphate ion. A tryptic dipeptide containing this essential cysteine was isolated following inactivation with iodo[2-14C]acetate.

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Accession: 006712234



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