用来自大肠杆菌A2菌株的细菌蛋白酶切割的肌动蛋白的物理化学性质。
Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain.
作者信息
Collins J H, Kuznetsova I M, Pershina V P, Synakevich I G, Turoverov K K, Usmanova A M
机构信息
Institute of Cytology, USSR Academy of Sciences, Leningrad.
出版信息
FEBS Lett. 1991 Feb 11;279(1):49-51. doi: 10.1016/0014-5793(91)80247-z.
The 36 kDa fragment of actin molecule obtained with the protease from E. coli A2 strain [(1988) FEBS Lett. 228, 172] was shown to begin with Val-43 and retain the COOH-terminal amino acid residues of the parent molecule. The E. coli protease split actin preserves the NH2-terminal part of the polypeptide chain as well as the native conformation of actin molecule. However, the E. coli protease split actin failed to polymerize in 0.1 M KCl, suggesting that integrity of actin molecule between Gly-42 and Val-43 is crucial for actin polymerization.
用来自大肠杆菌A2菌株的蛋白酶获得的肌动蛋白分子36 kDa片段[(1988)《欧洲生物化学学会联合会快报》228, 172]显示以Val-43起始，并保留了亲本分子的COOH末端氨基酸残基。经大肠杆菌蛋白酶切割的肌动蛋白保留了多肽链的NH2末端部分以及肌动蛋白分子的天然构象。然而，经大肠杆菌蛋白酶切割的肌动蛋白在0.1 M KCl中无法聚合，这表明肌动蛋白分子中Gly-42和Val-43之间的完整性对于肌动蛋白聚合至关重要。
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