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Identification of a connecting filament protein in insect fibrillar flight muscle

, : Identification of a connecting filament protein in insect fibrillar flight muscle. Journal of Molecular Biology 153(3): 661-680

A major component on sodium dodecyl sulfate-containing gels of solubilized isolated Z-discs, purified from honeybee flight muscle, migrates with an apparent MW of 360,000. Antibodies to this high MW polypeptide were prepared by injecting rabbits with homogenized gel slices containing the protein band. With indirect immunofluorescence microscopy these antibodies are localized to a region extending from the edge of the Z-band to the A-band in shortened or stretched sarcomeres. Glycerinated flight muscle treated with antiserum and prepared for EM shows enhanced density from the ends of the thick filaments to the I-Z junction regardless of sarcomere length. Antiserum is directed toward a structural protein of connecting filaments, which link thick filaments to the Z-band in insect fibrillar muscle, rather than to a thin filament component. In Ouchterlony double-diffusion experiments a single precipitin band is formed when antiserum is diffused against solubilized Z-discs; no reaction occurs between antiserum and proteins from native thin filaments prepared from honeybee light muscle. Antibody stains the I-band in flight muscle fibrils from which thin filaments are removed. Honeybee leg muscle myofibrils, in which connecting filaments are not observed, are not labeled with antibody. Since antibody binds to the short projections which extend from the flat surfaces of isolated Z-discs, these projections are assumed to be remnants of connecting filaments and the source of the 360,000 MW protein. The amino acid composition of this high MW material, purified by Sepharose chromatography, is presented. The protein was named projectin.


PMID: 6802982

DOI: 10.1016/0022-2836(81)90412-5

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