Primary structure of inhibitor-2 from rabbit skeletal muscle
نویسندگان
چکیده
منابع مشابه
Primary structure of rabbit skeletal muscle glycogen synthase deduced from cDNA clones.
The complete amino acid sequence of rabbit skeletal muscle glycogen synthase was deduced from cDNA clones with a composite length of 3317 bp. An mRNA of 3.6 kb was identified by Northern blot analysis of rabbit skeletal muscle RNA. The mRNA coded for a protein of 734 residues with a molecular weight of 83,480. The deduced NH2-terminal and COOH-terminal sequences corresponded to those reported f...
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We have isolated two overlapping 17-kilobase (kb) genomic clones which, together, encode the rabbit fast-twitch skeletal muscle calsequestrin. The calsequestrin gene is 8.6 kb in length and consists of 11 exons. S1 nuclease protection and primer extension analyses position the transcription initiation site 191 nucleotides upstream of the translation initiation codon. The 5'-flanking sequence co...
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The AMP-deaminases from chicken and rabbit muscle have been investigated by techniques which include sedimentation equilibrium, sodium dodecyl sulfate gel electrophoresis, amino acid analysis, NH2- and COOH-terminal analyses, and tryptic peptide mapping. The molecular weights of the native chicken (276,000) and rabbit (271,000) enzymes obtained by sedimentation equilibrium studies are in good a...
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Adenylosuccinate synthetase has been purified more than 250-fold from extracts of rabbit muscle acetone powder by heating to 60”, ammonium sulfate fractionation, phosphocellulose and hydroxylapatite chromatography, and Sephadex G-150 gel filtration. Crystals have been obtained by dialysis against 60 to 67% ammonium sulfate. Enzyme activity is stable for about 2 weeks in phosphate buffer contain...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1986
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1986.tb09474.x