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PMID: 3446177 Published · ppublish English Journal Article

Anti-actin antibodies. An immunological approach to the myosin-actin and the tropomyosin-actin interfaces.

The Biochemical journal ·Vol. 244 ·No. 3 ·1987-06-15 ·Pages 571-7

Mejean C, Boyer M, Labbé JP, Marlier L, Benyamin Y, Roustan C

Abstract

The topography of the rigor complex between subfragment-1 (S-1) of myosin and actin was investigated by using several specific antibodies directed to well-located sequences in actin. A major contact area for S-1 was characterized in the hydrophilic 18-28 constant sequence, and the variable 1-7 sequence was only found to be in close proximity to the interface. The C-terminal extremity of actin situated around Cys-374 appeared to be included in a region close to the S-1 heavy chain and the N-terminal part of actin. The interaction between tropomyosin and actin was also studied. Neither of the terminal parts of actin were involved in this interaction. Thus, the regions involved in the interactions of S-1 and tropomyosin with actin do not overlap.

MeSH Terms
Actins/immunology,metabolism Amino Acid Sequence Animals Antibodies Binding Sites Enzyme-Linked Immunosorbent Assay Macromolecular Substances Myosins/metabolism Peptide Fragments/metabolism Rabbits Tropomyosin/metabolism
Chemicals
Actins Antibodies Macromolecular Substances Peptide Fragments Tropomyosin Myosins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Mejean C
Centre de Recherches de Biochimie Macromoléculaire (CNRS), U 249 (INSERM), Université de Montpellier I, France.
Boyer M
Labbé J P
Marlier L
Benyamin Y
Roustan C
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2440571
Published
1987-06-15
Pages
571-7
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1148034
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2440571 PMC Full Text View journal details
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