COMPLETE AMINO-ACID-SEQUENCE OF THE CATALYTIC SUBUNIT OF BOVINE CARDIAC-MUSCLE CYCLIC AMP-DEPENDENT PROTEIN-KINASE
COMPLETE AMINO-ACID-SEQUENCE OF THE CATALYTIC SUBUNIT OF BOVINE CARDIAC-MUSCLE CYCLIC AMP-DEPENDENT PROTEIN-KINASE
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DOI：
10.1073/pnas.78.2.848
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发表时间：
1981-01-01
期刊：
影响因子：
--
通讯作者：
TITANI, K
中科院分区：
文献类型：
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作者：
SHOJI, S;PARMELEE, DC;TITANI, K
牛心肌cAMP依赖性蛋白激酶催化亚基的349个残基的完整氨基酸序列。该亚基的序列（MW 40，580，包括苏氨酸-196和丝氨酸-337处的磷酸基团）主要是通过用溴化氰切割甲硫氨酰键从羧甲基化蛋白质产生的9个片段的自动Edman降解而得。通过分析从体外放射性标记的蛋白质中分离的含甲硫氨酸的胰蛋白酶肽（通过甲硫氨酸残基的[14 C]甲基交换），将这些片段沿着多肽链排列。该分子仅在位置198和342处含有2个半胱氨酰残基。它是相对极性的，含有朝向氨基末端的阳离子残基簇和朝向羧基末端的阴离子残基簇。二级结构的预测表明存在3个主要结构域，其中大约一半的残基出现在α-螺旋和12%的β-股。
The complete amino acid sequence of the 349-residue catalytic subunit of cAMP-dependent protein kinase from bovine cardiac muscle is presented. The sequence of the subunit (MW 40,580 including phosphate groups at threonine-196 and serine-337) was derived largely by automated Edman degradation of 9 fragments generated from the carboxymethylated protein by cleavage of methionyl bonds with cyanogen bromide. These fragments were aligned along the polypeptide chain by analysis of methionine-containing tryptic peptides isolated from protein radiolabeled in vitro by [14C]methyl exchange at methionyl residues. The molecule contains only 2 cysteinyl residues, at positions 198 and 342. It is relatively polar, containing clusters of cationic residues toward the amino terminus and anionic residues towards the carboxyl terminus. Predictions of secondary structure suggest the presence of 3 major domains with approximately half of the residues occurring in .alpha.-helices and 12% in .beta.-strands.