Stoichiometry of covalent actin-subfragment 1 complexes formed on reaction with a zero-length crosslinking compound
- 1 May 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (10) , 2211-2214
- https://doi.org/10.1021/bi00305a017
Abstract
The interaction of actin and rabbit subfragment 1 has been reexamined by using a carbodiimide cross-linking reagent. A major doublet with an apparent MW of 134,000 as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis has been identified. A minor product of much higher MW is also formed. Stoichiometry determinations using [3H]actin and [14C]subfragment 1 indicate that the major doublet is a 1:1 complex of actin and subfragment 1. This result confirms that reported by Sutoh.This publication has 10 references indexed in Scilit:
- Mapping of actin-binding sites on the heavy chain of myosin subfragment 1Biochemistry, 1983
- Cross-linking of F-actin to skeletal muscle myosin subfragment 1 with bis(imido esters): further evidence for the interaction of myosin-head heavy chain with an actin dimerBiochemistry, 1982
- An actin-binding site on the 20K fragment of myosin subfragment 1Biochemistry, 1982
- Comparison of crosslinked and natural polypeptides as standards for molecular weight determination of large polypeptides (guinea pig thyroglobulin) by SDS-gel electrophoresisAnalytical Biochemistry, 1981
- Structure of the actin–myosin interfaceNature, 1981
- Proteolytic approach to structure and function of actin recognition site in myosin headsBiochemistry, 1981
- Liquid scintillation counting of polyacrylamide gels crosslinked with N,N′-methylene-bis-acrylamide and N,N′-diallyltartardiamideAnalytical Biochemistry, 1980
- Studies on the role of myosin alkali light chainsJournal of Molecular Biology, 1977
- Free Adenosine Diphosphate as an Intermediary in the Phosphorylation by Creatine Phosphate of Adenosine Diphosphate Bound to ActinJournal of Biological Chemistry, 1967
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951