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PMID: 4009727 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Electron microscopy of cross-linked scallop myosin.

Journal of molecular biology ·Vol. 183 ·No. 2 ·1985-05-25 ·Pages 283-6

Vibert P, Cohen C, Hardwicke PM, Szent-Györgyi AG

Abstract

The N-terminal regions of the regulatory light chains on the two heads of scallop myosin can be cross-linked to one another. Electron microscopy of cross-linked myosin molecules, and of dimers of myosin subfragment-1 produced by digesting them with papain, shows that the site of cross-linking is very close to the head-rod junction.

MeSH Terms
Animals Macromolecular Substances Microscopy, Electron Mollusca Myosin Subfragments Myosins Peptide Fragments
Chemicals
Macromolecular Substances Myosin Subfragments Peptide Fragments Myosins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Vibert P
Cohen C
Hardwicke P M
Szent-Györgyi A G
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
DOI
10.1016/0022-2836(85)90221-9
Published
1985-05-25
Pages
283-6
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Grants
NIADDK NIH HHS · AM15963 · United States
NIADDK NIH HHS · AM17346 · United States
External Links
PubMed source DOI: 10.1016/0022-2836(85)90221-9 View journal details
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