PMID: 108275May 25, 1979

Chicken parvalbumin. Comparison with parvalbumin-like protein and three other components (Mr = 8,000 to 13,000).

The Journal of Biological Chemistry
C W Heizmann, E E Strehler


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 myo...Continue Reading

Related Concepts

Amino Acids
Chick Embryo
Immunodiffusion Measurement
Molecular Weight
Muscle Proteins

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