Studies on the role of sulfhydryls in the myosin ATPase. Characterization of the site of modification by the bifunctional sulfhydryl reagent p-N,N'-phenylenedimaleimide.
作者： M. Burke , P.J. Knight
DOI: 10.1016/S0021-9258(18)43503-X
关键词: Chemistry 、 Sulfhydryl reagent 、 Cleavage (embryo) 、 Sequence analysis 、 Myosin 、 Biochemistry 、 Myosin ATPase 、 Covalent bond 、 Bifunctional 、 Peptide
摘要: Abstract Myosin has been modified with near stoichiometric amounts of the bifunctional reagent [14C]p-N,N'-phenylenedimaleimide (pPDM) in presence MgADP under conditions which abolish its ATPase activity. Subsequent carboxymethylation and CNBr cleavage results 14C label being associated a single polypeptide Mr approximately 10,000. Amino acid composition partial sequence analysis this peptide showed that it corresponded to containing -SH1 -SH2 sequenced by Elzinga Collins (Elzinga, M., Collins, J.H. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 4281-4284) labeled at or N-ethylmaleimide Kunz et al. (Kunz, P.A., Walser, J.T., Watterson, J.G., Schaub, M.C. FEBS Lett. 83, 137-140). These data indicating pPDM does -SH1- -SH2-containing region myosin covalently bridging them shows these thiols can approach within 12 14 A.
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