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• W1966375725 startingPage "3807" @default.
• W1966375725 abstract "Smooth muscle myosin heavy chains [SM1, approximately 205 kilodaltons (kDa), and SM2, approximately 200 kDa] were separated on sodium dodecyl sulfate (SDS)-polyacrylamide gels. Peptide maps of the two heavy chains showed unique patterns. Limited proteolytic cleavage of purified swine stomach myosin was performed by using a variety of proteases to produce the major myosin fragments which were resolved on SDS gels. A single band was obtained for heavy meromyosin in the soluble fraction following chymotrypsin digestion. However, a variable number of bands were observed for light meromyosin fragments in the insoluble fraction after chymotrypsin digestion. Peptide mapping indicated that the two bands observed after short digestion times with chymotrypsin had relative mobility and solubility properties consistent with approximately 100- and 95-kDa light meromyosin (LMM) fragments. These results indicate that the region of difference between SM1 and SM2 lies in the LMM fragment." @default.
• W1966375725 created "2016-06-24" @default.
• W1966375725 creator A5012885769 @default.
• W1966375725 creator A5078379123 @default.
• W1966375725 date "1988-05-01" @default.
• W1966375725 modified "2023-09-26" @default.
• W1966375725 title "Two smooth muscle myosin heavy chains differ in their light meromyosin fragment" @default.
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• W1966375725 doi "https://doi.org/10.1021/bi00410a043" @default.
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