A kinetic study of rabbit muscle pyruvate kinase
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چکیده
منابع مشابه
A kinetic study of muscle pyruvate kinase from Carcinus maenas.
mantle coincided with the time when the greatest shell shoot was measured (Table 1, day 40). Our results support the view that, at least in mantle tissue, there is a direct correlation between shell formation and carbonic anhydrase activity. A major function of the gill is gaseous exchange, and the fact that gill carbonic anhydrase activity follows a similar pattern of change to that of new she...
متن کاملSubunit structure of rabbit muscle pyruvate kinase.
Peptide mapping of rabbit muscle pyruvate kinase following tryptic digestion gave one-quarter the number of ninhydrin-reactive peptides, arginine-containing peptides, and tryptophan-containing peptides expected from the amino acid composition. Sedimentation velocity studies and disc gel electrophoresis of the enzyme subunits formed in 4 M urea and having one-quarter of the initial molecular wei...
متن کاملA kinetic analysis of rabbit muscle pyruvate kinase in the reverse direction.
For a complete kinetic analysis of an enzyme the reaction should be studied in both directions as only in this way can sufficient information about the enzyme complexes formed be obtained. In recent years several kinetic studies of the forward reaction of rabbit muscle pyruvate kinase have been made (Reynard et al., 1961; Ainsworth & MacFarlane, 1973) but no systematic studies of the reverse re...
متن کاملKinetic studies on the regulation of rabbit liver pyruvate kinase.
Two kinetically distinct forms of pyruvate kinase (EC 2.7.1.40) were isolated from rabbit liver by using differential ammonium sulphate fractionation. The L or liver form, which is allosterically activated by fructose 1,6-diphosphate, was partially purified by DEAE-cellulose chromatography to give a maximum specific activity of 20 units/mg. The L form was allosterically activated by K(+) and op...
متن کاملReversible solvent denaturation of rabbit muscle pyruvate kinase.
The structural transitions of the tetrameric rabbit muscle pyruvate kinase induced by guanidine hydrochloride and urea are characterized by elastic and quasi-elastic light-scattering, sedimentation velocity, and intrinsic viscosity experiments as well as by protein fluorescence, circular dichroism, and enzymic activity measurements. The transition curves are shown to be reversible. We find a ne...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1973
ISSN: 0264-6021
DOI: 10.1042/bj1310223