Cellular distribution of sarcoplasmic calcium-binding proteins by immunofluorescence.
Specific antibodies against carp paravalbumin, crayfish calcium binding protein and crayfish arginine kinase were used for indirect immunofluorescence localization of the respective proteins. Simultaneous staining of the same muscle sections with human serum containing anti-actin autoantibodies served as a probe to identify the isotropic band. Parvalbumin appears to be evenly distributed in carp white muscle. The crayfish calcium binding protein however shows a distinct localization, in the isotropic band, coincident with the actin staining. Arginine kinase, which has the same molecular weight and is extractible in the same way as the calcium binding protein does not show this distinct localization, but is evenly present in crayfish tail muscle, similarly to parvalbumin. The possible meaning of the different distribution of the two calcium binding proteins is discussed.
D000818:Animals; D001120:Arginine; D003400:Astacoidea; D002118:Calcium / Q000378:metabolism*; D002347:Carps; D002352:Carrier Proteins / Q000032:analysis*; D005455:Fluorescent Antibody Technique; D009124:Muscle Proteins / Q000378:metabolism*; D009132:Muscles / Q000032:analysis*; D010320:Parvalbumins / Q000032:analysis; D010770:Phosphotransferases / Q000032:analysis; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D002352:Carrier Proteins; D009124:Muscle Proteins; D010320:Parvalbumins; D001120:Arginine; D010770:Phosphotransferases; D002118:Calcium