Measurement of the fraction of myosin heads bound to actin in rabbit skeletal myofibrils in rigor.
Measurement of the fraction of myosin heads bound to actin in rabbit skeletal myofibrils in rigor.
复制标题
测量兔骨骼肌原纤维中与肌动蛋白结合的肌球蛋白头部的分数。
DOI:
10.1016/0022-2836(81)90352-1
复制
发表时间:
1981
影响因子:
5.6
通讯作者:
Harrington,WF
中科院分区:
文献类型:
--
作者:
Lovell,SJ;Harrington,WF
Tryptic digestion of rabbit skeletal myofibrils at physiological ionic strength and pH results in cleavage of the myosin heavy chain at one site giving two bands (Mr= 200,000 and 26,000) on sodium dodecyl sulfate/polyacrylamide gels. Following addition of sodium pyrophosphate (to 1 mm) to dissociate the myosin heads from actin, tryptic proteolysis results in production of three bands, 160K†, 51K and 26K, with a 74K band appearing as a precursor of the 51K and 26K species. Under these conditions, there is insignificant cleavage of heavy chain to the heavy and light meromyosins. Trypsin-digested myofibrils yield the same amount of rod as native myofibrils when digested with papain. These results indicate that actin blocks tryptic cleavage of the myosin heavy chain at a site 74K from the N terminus. From measurements of the amount of 51K species formed by digestion of rigor fibers at various sarcomere lengths, we estimate that at least 95% of the myosin heads are bound to actin at 100% overlap of thick and thin filaments. Hence all myosin molecules can bind to actin, and consequently both heads of a myosin molecule can interact simultaneously with actin filaments under rigor conditions.
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影响因子:
5.6
作者:
HUXLEY, HE;BROWN, W
通讯作者:
BROWN, W
影响因子:
3.9
作者:
J. Potter
通讯作者:
J. Potter
影响因子:
5.6
作者:
K. Sutoh;T. Karr;W. F. Harrington
通讯作者:
W. F. Harrington
DOI:
10.1016/s0021-9258(18)93820-2
发表时间:
1964
期刊:
The Journal of biological chemistry
影响因子:
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作者:
D. Young;S. Himmelfarb;W. F. Harrington
通讯作者:
W. F. Harrington
DOI:
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发表时间:
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期刊:
影响因子:
--
作者:
通讯作者:
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