Two Smooth Muscle Myosin Heavy Chains Differ in Their Light Meromyosin Fragment

Document Type

Article

Language

eng

Format of Original

5 p.

Publication Date

5-1988

Publisher

American Chemical Society

Source Publication

Biochemistry

Source ISSN

0006-2960

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.

Comments

Biochemistry, Vol. 27, No. 10 (May 1988): 3807-3811. DOI.

Thomas Eddinger was affiliated with the University of Virginia at the time of publication.

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