Effect of the integrity of the myofibrillar structure on the tryptic accessibility of a hinge region of the myosin rod

FEBS Letters

Muhlrad, Andras¹  Assulin, Olga³  Werber, Moshe M.² 

[1] Department of Oral Biology, Hebrew University-Hadassah School of Dental Medicine, Jerusalem, Israel;Department of Medical Laboratories, Meir Hospital, Kfar Sava, Israel;Polymer Research Department, Weizmann Institute of Science, Rehovot, Israel

关键词: Myofibrillar structure Myosin hinge region Tryptic proteolysis;    DTT;    1;    4-dithiothreitol;    HMM;    heavy meromyosin;    1;    5-IAEDANS;    5-iodoacetamidoethylaminonaphthalene-1-sulfonic acid;    LMM;    light meromyosin;    S-1;    heavy meromyosin subfragment-1;    S-2;    heavy meromyosin subfragment-2;   

DOI  :  10.1016/0014-5793(86)80351-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Limited proteolysis has been used to study the influence of actin, in the absence or presence of regulatory proteins of the thin filament (tropomyosin and troponin), as well as that of the myofibrillar structure on the tryptic cleavage of the heavy meromyosin (HMM)/light meromyosin (LMM) hinge region in myosin heavy chain. Cleavage at the HMM/LMM hinge is almost absent in myofibrils, whereas this hinge is accessible to tryptic digestion in actomyosin, in native thin filaments attached to myosin and in myosin heavy chain alone. This observation indicates that it is the myofibrillar structure which profoundly affects the tryptic accessibility of this specific hinge region of myosin. This provides a good example of the manner by which a highly organized supramolecular structure might affect the chemical properties of a specific site in a macromolecule.

【 授权许可】

Unknown