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Biochem Biophys Res Commun. 1994 Feb 28;199(1):56-62.

Carp parvalbumin binds to and directly interacts with the sarcoplasmic reticulum for Ca2+ translocation.

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Laboratory of Marine Biochemistry, Faculty of Agriculture, University of Tokyo, Japan.


Interaction between two relaxing factors, the sarcoplasmic reticulum and parvalbumin, in carp fast skeletal muscle was investigated. Immunoblotting using an anti-parvalbumin antibody revealed that parvalbumin bound to the light sarcoplasmic reticulum isolated from carp fast skeletal muscle in the presence of Ca2+. Parvalbumin enhanced Ca2+ uptake activity of the light sarcoplasmic reticulum. Furthermore, using a photoreactive cross-linker, we detected a protein in the light sarcoplasmic reticulum which bound to parvalbumin in a Ca(2+)-dependent manner. These results suggest that parvalbumin may directly interact with the sarcoplasmic reticulum in contraction-relaxation cycle of carp fast skeletal muscle.

[Indexed for MEDLINE]

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