Primary structure of chicken muscle pyruvate kinase mRNA.
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 کاملThe primary structure of chicken B-creatine kinase and evidence for heterogeneity of its mRNA.
cDNA clones for chicken B-CK were isolated by immunoscreening from a gizzard cDNA library constructed in the expression vector lambda gtll. The entire coding portion in addition to the complete 3' untranslated region and 42 bp of the 5' noncoding part are represented in the clone H4. On RNA blots H4 insert DNA hybridized to a 1600 bp poly(A)+ RNA from gizzard, brain and heart but not to breast ...
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 کاملRegulatory Properties of Skeletal-Muscle Pyruvate Kinase
Hitherto it has been generally supposed that pyruvate kinase (EC 2.7.1.40) has no significant role in the regulation in vivo of glycolytic flux in skeletal muscle (Carbonell et al., 1973). This supposition, apart from providing an explanation for the apparent lack of potentially regulatory allosteric interactions by skeletal-muscle (M-type) pyruvate kinase, is in agreement with the idea that gl...
متن کاملL-Phenylalanine inhibition of muscle pyruvate kinase.
The allosteric inhibition of M1-type pyruvate kinase from rabbit skeletal muscle by phenylalanine is reciprocally dependent on Mg2+ and phosphoenolpyruvate concentrations. At pH 8, phenylalanine acts as a competitive inhibitor with respect to Mg2+ and phosphoenolpyruvate, and vice versa. Phenylalanine introduces sigmoidicity into the dependence of the reaction velocity on [Mg2+]. In vitro kinet...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1983
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.80.12.3661