在核苷酸存在的情况下，经胰蛋白酶消化后，肌球蛋白亚片段-1的热稳定性降低。

Thermal stability of myosin subfragment-1 decreases upon tryptic digestion in the presence of nucleotides.

作者信息

Pintér K, Lu R C, Szilágyi L

出版信息

FEBS Lett. 1986 May 5;200(1):221-5. doi: 10.1016/0014-5793(86)80542-7.

Abstract

Myosin subfragment-1 (S-1), digested with trypsin in the presence of ATP, rapidly loses its ATPase activity upon mild heat treatment even if ATP or ADP is present. The heat-treated molecule is very sensitive to further tryptic digestion. Undigested S-1 and S-1 digested in the absence of ATP are protected by nucleotides. The loss of the protective effect of nucleotides correlates with the tryptic splitting of the 25 kDa amino-terminal fragment between Arg 23 and Ile 24.

摘要

肌球蛋白亚片段1（S-1）在ATP存在的情况下用胰蛋白酶消化，即使存在ATP或ADP，经温和热处理后也会迅速丧失其ATP酶活性。热处理后的分子对进一步的胰蛋白酶消化非常敏感。未消化的S-1和在无ATP情况下消化的S-1受到核苷酸的保护。核苷酸保护作用的丧失与25 kDa氨基末端片段在精氨酸23和异亮氨酸24之间的胰蛋白酶裂解有关。