ELECTROPHORETIC AND IMMUNOLOGICAL STUDIES ON THE LIGHT CHAINS OF MYOSIN

概要

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Myosin was highly purified mainly by combining procedures of ammonium sulfate fractionation and chromatographies on cellulose phosphate, DEAE-cellulose and DEAE-Sephadex A-50 as judged by gel electrophoresis and immunological analyses. The highly purified myosin produced two precipitin lines in immunodiffusion with antibodies to myosin, whereas the myosin produced only one peak in quantitative precipitin analysis. This difference implied the possibility that agar gel promoted the dissociation of light chains from myosin. Immunological analyses of light chains prepared from the myosin showed the presence of two kinds of light chain components. On the other hand, light chains were separated usually into two components, L-1 (molecular weight 27,000) and L-2 (mol. wt. 17,000) in SDS-gel electrophoresis. However, an additional component, L-3 (mol. wt. 14,000) was sometimes appeared in the electrophoresis of light chains. The possibility that L-3 was a breakdown product of L-1 was discussed.
北海道大学の論文