Procedures for a rapid isolation and purification of parvalbumin (Mr = 12,600), parvalbumin-like protein (Mr = 12,800), and three other polypeptides with molecular weights of 12,400 (Component 1), 11,700 (Component 2), and 8,000, respectively, from chicken leg muscle, are described. A direct comparison of parvalbumin with these other proteins showed distinct differences in the amino acid compositions, charge, and immunological behavior. Parvalbumin has two high affinity sites for Ca2+ with a KDiss less than or equal to 10(-6) M (Blum, H. E., Lehky, P., Kohler, L., Stein, E.A., and Fischer, E. H. (1977) J. Biol. Chem. 252, 2834-2838), in contrast to parvalbumin-like protein. Components 1 and 2, and the Mr = 8,000 protein, where only low affinity sites for Ca2+ could be detected (KDiss greater than 10(-3) M). From our results it is concluded that the co-extracted proteins do not constitute isoproteins of parvalbumin. The very low affinity for Ca2+ suggests that these proteins are not involved in processes of Ca2+ transport or Ca2+ regulation as proposed for parvalbumin. Parvalbumin could not be localized within isolated myofibrils and also did not accumulate in primary myogenic cell cultures together with proteins forming the myofibrillar structure. Parvalbumin was not even detected in myotubes in which myofibrils and sarcoplasmatic reticulum were already assembled and functioning. Parvalbumin (or cross-reacting material) was detected in leg muscle and brain 1 day after hatching of the chick. Possible roles for parvalbumin are discussed.
|Original language||English (US)|
|Number of pages||8|
|Journal||Journal of Biological Chemistry|
|State||Published - May 25 1979|
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