Fate of the light chains in the course of proteolytic digestion of rabbit fast skeletal myosin
Author:
Publisher
Elsevier BV
Subject
General Medicine,Biochemistry
Reference26 articles.
1. The adenosinetriphosphatase activity of myofibrils isolated from skeletal muscle
2. FRAGMENTATION OF MYOSIN BY CHYMOTRYPSIN
3. TRYPSIN DIGESTION OF MUSCLE PROTEINS
4. TRYPSIN DIGESTION OF MUSCLE PROTEINS
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1. ‘Artificial’ Myosin Isozymes; Preparation and Characteristics;European Journal of Biochemistry;2005-03-03
2. Cleavage points of rabbit skeletal myosin light chains selectively modified in situ by limited proteolysis: structural characteristics of the neoformed isozymes;FEBS Letters;1995-08-07
3. Regulatory light chain influences alterations of myosin head induced by actin;FEBS Letters;1991-12-16
4. Possible presence of the difference peptide in alkali light chain 1 of fish fast skeletal myosin;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1990-01
5. Temperature-dependent conformational transition in the head-rod junctional region of the myosin molecule;European Journal of Biochemistry;1988-11
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