PMID: 708767Sep 26, 1978Paper

Parvalbumins from coelacanth muscle. III. Amino acid sequence of the major component

Biochimica Et Biophysica Acta
J Jauregui-Adell, J F Pechere


The primary structure of the major parvalbumin (pI = 4.52) from coelacanth muscle (Latimeria chalumnae) has been determined. Sequence analysis of the tryptic peptides, in some cases obtained with beta-trypsin, accounts for the total amino acid content of the protein. Chymotryptic peptides provide appropriate sequence overlaps, to complete the localization of the tryptic peptides. Examination of the amino acid sequence of this protein shows the typical structure of a beta-parvalbumin. Its position in the dendrogram of related calcium-binding proteins corresponds to that usually accepted for crossopterygians.


Apr 29, 1977·Journal of Molecular Evolution·M Goodman, J F Pechere
Apr 1, 1975·Proceedings of the National Academy of Sciences of the United States of America·D L EnfieldH Neurath
Oct 1, 1973·Archives of Biochemistry and Biophysics·R A Beardslee, J C Zahnley


Jun 1, 1990·Journal of Molecular Evolution·N D MoncriefM Goodman
Nov 8, 1994·Proceedings of the National Academy of Sciences of the United States of America·U A BetzJ Klein
Jan 1, 1979·Biochimie·C GerdayG Hamoir
Apr 1, 1982·European Journal of Biochemistry·J Jauregui-AdellJ Demaille
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Jan 25, 2017·Clinical and Experimental Allergy : Journal of the British Society for Allergy and Clinical Immunology·J N StephenA L Lopata
Jul 1, 1988·European Journal of Biochemistry·T KobayashiY Watanabe
Sep 1, 1993·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·S KomatsuH Hirano
Mar 1, 1983·European Journal of Biochemistry·W Wnuk, J Jauregui-Adell

Related Concepts

Muscle Proteins
Peptide Fragments

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