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Anti-actin antibodies: immunological approach to the myosin and the tropomyosin-actin interface

Academic Article
Publication Date:
1987
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.
Iris type:
01.01 Articolo in rivista
List of contributors:
Marlier, LIONEL JEANLUC NORBERT
Authors of the University:
MARLIER LIONEL JEANLUC NORBERT
Handle:
https://iris.cnr.it/handle/20.500.14243/140895
Published in:
BIOCHEMICAL JOURNAL (LOND., 1984)
Journal
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