3-METHYLHISTIDINE IN ACTIN AND OTHER MUSCLE PROTEINS
3-METHYLHISTIDINE IN ACTIN AND OTHER MUSCLE PROTEINS
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DOI：
10.1042/bj1050361
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发表时间：
1967-01-01
影响因子：
4.1
通讯作者：
PERRY, SV
中科院分区：
文献类型：
--
作者：
JOHNSON, P;HARRIS, CI;PERRY, SV
应用扩展洗脱系统对哺乳动物、鱼类和鸟类骨骼肌肌动蛋白水解产物进行碱性氨基酸分析，检测到3-甲基组氨酸。证据表明，3-甲基组氨酸的形式的一级结构的一部分，在兔肌动蛋白这一残基被限制到1肽馏分从胰蛋白酶消化。兔骨骼肌肌动蛋白的3-甲基组氨酸与组氨酸的比例为1：7.6，表明其最小分子量为47，600。成年兔肌球蛋白含有约2，3-甲基组氨酸残基/mol。这些残基位于分子的重酶解肌球蛋白部分，并限于琥珀酰化后获得的主要组分。
By the use of the extended elution system for basic amino acid analysis, 3-methylhistidine was detected in hydrolysates of actin isolated from mammalian, fish and bird skeletal muscle. Evidence is presented to indicate that 3-methylhistidine forms part of the primary structure and that in rabbit actin this residue is restricted to 1 peptide fraction obtained from the tryptic digest. Rabbit skeletal muscle actin has a 3-methylhistidine histidine ratio 1:7.6, indicating a minimum molecular weight of 47,600. Adult rabbit myosin contains approximately 2,3-methylhistidine residues/mol. These residues are localized in the heavy meromyosin part of the molecule, and are restricted to the major component obtained after succinylation.