The binding of myosin heads on heavy meromyosin and assembled myosin to actin in the presence of nucleotides. Measurements by the proteolytic rates method.-Reference-Cited by-同舟云学术

The binding of myosin heads on heavy meromyosin and assembled myosin to actin in the presence of nucleotides. Measurements by the proteolytic rates method.

Published:1987-03 Issue:9 Volume:262 Page:4129-4133
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Duong A.M.,Reisler E.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference29 articles.

1. Tryptic cleavage and substructure of bovine cardiac myosin subfragment 1

2. Kinetic rates of tryptic digestion of bovine cardiac myofibrils. An improved measurement of cross-bridge dissociation.

3. Location of SH-1 and SH-2 in the heavy chain segment of heavy meromyosin

4. Effect of the filamentous structure of myosin on the actomyosin ATPase activity

5. Cross-bridge orientation in skeletal muscle measured by linear dichroism of an extrinsic chromophore

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1. Rescue of in vitro actin motility halted at high ionic strength by reduction of ATP to submicromolar levels;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1996-11

2. Relationship between cytosolic calcium and oxygen consumption in isolated rat hearts;Cell Calcium;1992-04

3. Interaction of Actin 1–28 with Myosin and Troponin I and the Importance of These Interactions to Muscle Regulation;Peptides as Probes in Muscle Research;1991

4. Electrostatic contributions to the binding of myosin and myosin-magnesium-ADP to F-actin in solution;Biochemistry;1990-11-01

5. Nucleotide-induced states of myosin subfragment 1 cross-linked to actin;Biochemistry;1989-04-18