Pyruvate kinase from human skeletal muscle.

Abstract:

:A simple method is described for the isolation of crystalline pyruvate kinase from human skeletal muscle. The enzyme was purified by ammonium sulfate fractionation, heat treatment and crystallization. Two crystal forms of pyruvate kinase differing in solubility but not in specific activity were found. The homogenous enzyme preparations in triethanolamine buffer, pH 7.6 reveal at 25 degrees a specific activity of 245 U per mg protein, and of 340 U/mg in potassium phosphate buffer (50 mM). The enzyme is activated by inorganic phosphate and fructosediphosphate to the same extent, and inhibited non competetively by ammonium ion. The molecular weight as measured by gel filtration is 220,000 daltons and the enzyme molecule is composed of 4 subunits.

journal_name

Mol Cell Biochem

authors

Baranowska B,Baranowski T

doi

10.1007/BF01732078

subject

Has Abstract

pub_date

1975-03-27 00:00:00

pages

197-201

issue

3

eissn

0300-8177

issn

1573-4919

journal_volume

6

pub_type

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