Refined purification and characterization of Z-protein.
Using an improved procedure, Z-protein was prepared from myofibrils of chicken breast muscle. The yield of pure Z-protein increased to 10 mg per kg of muscle. The chain weight of Z-protein was 55,000 in the presence of SDS. However, Z-protein was eluted before aldolase (Mr 158,000) in Sephacryl S-400 column chromatography, and, therefore, it appeared to exist as a tetramer in a physiological salt solution. Z-protein had at least four isopeptides whose isoelectric points ranged from pH 6.0 to 6.4. Anti-Z-protein antiserum reacted equally with these isopeptides. The extinction coefficient of Z-protein at wavelength 278 nm was 4.2 (1%; light path, 1 cm). Z-protein which was purified according to this improved method did not bind to F-actin and alpha-actinin in a physiological salt solution.
Department of Biology, Faculty of Science, Chiba University.
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Ohashi
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Maruyama
D000818:Animals; D030161:Avian Proteins; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens; D002852:Chromatography, Ion Exchange / Q000379:methods; D007526:Isoelectric Point; D008970:Molecular Weight; D009124:Muscle Proteins / Q000302:isolation & purification*; D013056:Spectrophotometry, Ultraviolet
D030161:Avian Proteins; D009124:Muscle Proteins; C036203:Z-protein (muscle), chicken