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THERMAL-DENATURATION OF THE ALKALI LIGHT CHAIN-20 KDA FRAGMENT-COMPLEX OBTAINED FROM MYOSIN SUBFRAGMENT-1

被引：12
作者：
GOLITSINA, NL
SHNYROV, VL
LEVITSKY, DI
机构：
[1] AN BAKH BIOCHEM INST, LENINSKY PROSPECT 33, MOSCOW 117071, USSR
[2] AN BELOZERSKY PHYSICOCHEM BIOL INST, MOSCOW 119899, USSR
[3] ACAD SCI USSR, INST THEORET & EXPTL BIOPHYS, PUSHCHINO 142292, USSR
来源：
FEBS LETTERS | 1992年 / 303卷 / 2-3期
基金：
美国国家科学基金会;
关键词：
MYOSIN SUBFRAGMENT-1; DOMAIN STRUCTURE; SCANNING MICROCALORIMETRY; RABBIT SKELETAL MUSCLE;
D O I：
10.1016/0014-5793(92)80532-L
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The thermal denaturation of the myosin subfragment 1 (S1) from rabbit skeletal muscle and of its derivatives obtained by tryptic digestion has been studied by means of differential scanning calorimetry. Two distinct thermal transitions were revealed in the isolated complex of the C-terminal 20 kDa fragment of the S1 heavy chain with the alkali light chain. These transitions were identified by means of a thermal gel analysis method. It has been shown that the thermal denaturation of the 20 kDa fragment of the S1 heavy chain correlates with the melting of the most thermostable domain in the S1 molecule. It is concluded that this domain is located in the C-terminal 20 kDa segment of the S1 heavy chain.
引用
收藏
页码：255 / 257
页数：3
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