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J. Biochem, 1988, Vol. 103, No. 2 367-369
© 1988 Japanese Biochemical Society

research-article

FITC-Labeled I-Protein Specifically Binds to A-Bands and/or Z-Lines of Glycerinated Myofibrils of Chicken Breast Muscle1

Kazuyo Ohashi, Faculty of Science, Kensuke Ishikawa, Faculty of Science and Koscak Maruyama, Faculty of Science

Department of Biology,Chiba University Chiba, Chiba 260

Ion-exchange column-purified I-protein was labeled by fluorescein isothiocyanate (FITC) at an equimolar ratio. When FITC-labeled I-protein was reacted with glycerinated myofibrils of chicken breast muscle in a phosphate-buffered saline, fluorescence was observed at the A-band and/or the Z-line of the sarcomere. However, FITC-labeled I-protein did not stain freshly prepared myofibrils. When FITC-I-protein was reacted with a nitrocellulose paper sheet on which muscle proteins were blotted after SDS-poly aerylamide gel electrophoresis, some peptide bands, including connectin and nebulin, were fluorescent. These facts can explain why anti-I-protein antibodies stain the A-I junctional region of fresh myofibrils and A-bands and/or Z-lines of glycerinated myofibrils. It is very likely that I-protein is transferred from the A-I junctions of myofibrils and translocates to A-bands and Z-lines, where some components that can bind to I-protein are localized, as myofibrils are degraded during the glycerination.

1 This work was supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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