Title : Modification of thiols of gizzard myosin alters ATPase activity, stability of myosin filaments, and the 6-10 S conformational transition.

Pub. Date : 1985 Jan 10

PMID : 3155516






7 Functional Relationships(s)
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1 Modification of thiols of gizzard myosin alters ATPase activity, stability of myosin filaments, and the 6-10 S conformational transition. Sulfhydryl Compounds myosin heavy chain 14 Homo sapiens
2 Modification of thiols of gizzard myosin alters ATPase activity, stability of myosin filaments, and the 6-10 S conformational transition. Sulfhydryl Compounds myosin heavy chain 14 Homo sapiens
3 The pattern of incorporation of [14C]N-ethylmaleimide (MalNEt) into gizzard myosin indicates the presence of two classes of thiols: rapidly and slowly modified. Sulfhydryl Compounds myosin heavy chain 14 Homo sapiens
4 The first class contains two thiol residues, SH-A and SH-B, located in the myosin rod and the 17-kDa light chain, respectively, while the second contains at least two thiols located in the myosin heavy chain. Sulfhydryl Compounds myosin heavy chain 14 Homo sapiens
5 Modification of the second class of thiols is accompanied by a decrease in K+-EDTA-activated activity and an increase in Ca2+-activated activity measured above 0.3 M NaCl, where myosin neither forms filaments nor assumes the 10 S conformation. Sulfhydryl Compounds myosin heavy chain 14 Homo sapiens
6 These slow changes are characteristic of blocking the SH-1 thiols of skeletal-muscle myosin, but in gizzard myosin are attributable to modification of a less reactive thiol, SH-C. Sulfhydryl Compounds myosin heavy chain 14 Homo sapiens
7 These slow changes are characteristic of blocking the SH-1 thiols of skeletal-muscle myosin, but in gizzard myosin are attributable to modification of a less reactive thiol, SH-C. Sulfhydryl Compounds myosin heavy chain 14 Homo sapiens