M BAND PROTEIN

Author:

Eaton Barbra L.1,Pepe Frank A.1

Affiliation:

1. From the Biochemistry Graduate Group and the Department of Anatomy, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104

Abstract

M band protein can be specifically extracted from fresh chicken breast muscle myofibrils suspended in 5 mM Tris-HCl pH 8.0. During discontinuous polyacrylamide gel electrophoresis the isolated protein separates into three bands which can be identified as two separate components (A, B) and a complex of the two. When partially purified fractions of the separated components are combined, an increase in the intensity of the band containing the complex can be shown. The polypeptide chain weights of the two components are 100,000 (A) and 40,000 (B) daltons as estimated by sodium dodecyl sulfate- (SDS-) polyacrylamide gel electrophoresis. Antibody prepared against total M band protein stains only the M band of the myofibril and is completely absorbed by M band protein. M band protein also absorbs the M band staining specifically from antibody which stains both I and M bands. Immunodiffusion data indicate that anti-M band is a mixture of two specific antibodies, one against each component.

Publisher

Rockefeller University Press

Subject

Cell Biology

Cited by 48 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Isolation and characterization of distinct domains of sarcolemma and T-tubules from rat skeletal muscle;Biochemical Journal;1995-04-01

2. Cellular and molecular diversities of mammalian skeletal muscle fibers;Reviews of Physiology, Biochemistry and Pharmacology;1990

3. Fine structure of the A-band in cryo-sections diversity of M-band structure in chicken breast muscle;Journal of Ultrastructure and Molecular Structure Research;1988-07

4. Structure of the M Band;Journal of Electron Microscopy Technique;1987-06

5. Functionality of muscle proteins in gelation mechanisms of structured meat products;C R C Critical Reviews in Food Science and Nutrition;1985-01

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