PROPERTIES OF CRYSTALLINE PHOSPHORYLASE b
نویسندگان
چکیده
منابع مشابه
Some Properties of Cardiac Phosphorylase B Kinase.
Phosphorylase 6 kinase, the enzyme which catalyzes the conversion of phosphorylase b to phosphorylase a, has been extensively studied in extracts of skeletal muscle. Krebs, Graves, and Fischer (1) have reported that this enzyme exists in crude muscle extracts in a form that has very low activity at pH 7 and below. Above pH 7 the activity rises sharply with a maximum at pH 8.5. The enzyme with t...
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Lobster muscle phosphorylsse, in common with the phosphorylases of many other animal species, occurs in forms with different requirements for activity (1). Phosphorylase a is an active form; whereas phosphorylase 6 is active only in the presence of adenylic acid (AMP). It has been demonstrated with enzymes from mammalian species that phosphorylase may be converted from one form to another by re...
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In 1903 Hopkins and Cole (1) identified tryptophan as the source of indole produced by bacterial cultures. The tryptophan-inducible enzyme responsible for this conversion, which is found most commonly in Escherichia coli, was subsequently named tryptophanase by Happold and Hoyle (2). Wood, Gunsalus, and Umbreit (3) showed that tryptophanase catalyzed the stoichiometric conversion of tryptophan ...
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Nonactivated, partially purified bovine heart phosphorylase b kinase was activated by incubation with adenosine triphosphate and Mg+f ion prior to assay. Adenosine 3’ ,5’-cyclic pgosphate increased the rate of activation, but there was no absolute requirement for the cyclic nucleotide. Activation was particularly prominent when the subsequent assay for kinase activity was carried out at pH 7.0,...
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The kinetic properties of a glutaraldehyde-modified phosphorylase b have been examined to understand further the mechanism of allosteric transition of this enzyme. The sigmoidal response to AMP, which is observed with native glycogen phosphorylase b, cannot be demonstrated with the modified enzyme. This enzyme derivative also exhibits no homotropic cooperativity of glucose 1 -phosphate under co...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1958
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)70418-3