Subunit Structure of Rabbit Muscle Pyruvate Kinase
نویسندگان
چکیده
منابع مشابه
Subunit 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 کاملStructure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate.
The molecular structure of rabbit muscle pyruvate kinase, crystallized as a complex with Mn2+, K+, and pyruvate, has been solved to 2.9-A resolution. Crystals employed in the investigation belonged to the space group P1 and had unit cell dimensions a = 83.6 A, b = 109.9 A, c = 146.8 A, alpha = 94.9 degrees, beta = 93.6 degrees, and gamma = 112.3 degrees. There were two tetramers in the asymmetr...
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...
متن کاملThe refolding of denatured rabbit muscle pyruvate kinase.
The refolding of rabbit muscle pyruvate kinase after denaturation by guanidine hydrochloride was studied. On dilution of the denaturing agent, enzyme activity is only partially regained. The extent of regain of activity is dependent on protein concentration, showing a marked decrease at higher concentrations. The failure to regain complete activity appears to be related to the formation of inac...
متن کاملPhosphocreatine does not inhibit rabbit muscle phosphofructokinase or pyruvate kinase.
Certain phosphocreatine preparations contain a contaminant that inhibits phosphofructokinase and pyruvate kinase assays. The contaminant can be separated from phosphocreatine by anion exchange chromatography. After appropriate purification, phosphocreatine has no effect on phosphofructokinase or pyruvate kinase; thus, there is no evidence that it serves muscle as a regulator of these enzymes. A...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)91785-0