Anti-actin antibodies. An immunological approach to the myosin-actin and the tropomyosin-actin interfaces.
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.
Mejean
C
C
Centre de Recherches de Biochimie Macromoléculaire (CNRS), U 249 (INSERM), Université de Montpellier I, France.
Boyer
M
M
Labbé
J P
JP
Marlier
L
L
Benyamin
Y
Y
Roustan
C
C
D000199:Actins / Q000276:immunology / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D001665:Binding Sites; D004797:Enzyme-Linked Immunosorbent Assay; D046911:Macromolecular Substances; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D011817:Rabbits; D014335:Tropomyosin / Q000378:metabolism*
D000199:Actins; D000906:Antibodies; D046911:Macromolecular Substances; D010446:Peptide Fragments; D014335:Tropomyosin; D009218:Myosins