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J Cell Biol 1987 Apr 01;1044:841-7.
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Expression of the Ca2+-binding protein, parvalbumin, during embryonic development of the frog, Xenopus laevis.

Kay BK , Shah AJ , Halstead WE .

A cDNA segment encoding the Ca2+-binding protein, parvalbumin, was isolated with the use of antibodies, from a lambda gtll expression library of Xenopus laevis tadpole poly(A)+ RNAs. The bacterially expressed beta-galactosidase-parvalbumin fusion protein of one lambda recombinant shows high affinity 45Ca2+ binding. The sequence of the tadpole parvalbumin is highly similar to previously characterized beta-parvalbumins of other organisms. Data from protein and RNA blotting experiments demonstrate that parvalbumin is absent in oocytes, eggs, and early staged embryos, and only becomes expressed during embryogenesis at the time of myogenesis. The protein can be detected in individual developing muscle cells and in muscle fibers of tadpole tail muscles. A simple method is also described for the isolation of neural tube-notochord-somite complexes from Xenopus embryos.

PubMed ID: 3558484
PMC ID: PMC2114428

Species referenced: Xenopus laevis
Genes referenced: mindy3 ocm3 ocm4.2 ocm4.5
Antibodies: Ocm Ab1

Article Images: [+] show captions
References [+] :
Berchtold, Primary structure of parvalbumin from rat skeletal muscle. 1982, Pubmed