The amino acid sequence of porcine intestinal calcium-binding protein

1979 ◽  
Vol 57 (6) ◽  
pp. 737-748 ◽  
Author(s):  
Theo Hofmann ◽  
Michiko Kawakami ◽  
Anthony J. W. Hitchman ◽  
Joan E. Harrison ◽  
Keith J. Dorrington
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intestinal Mucosa ◽  
Calcium Binding ◽  
Binding Protein ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

The complete amino acid sequence of the calcium-binding protein (CaBP) from pig intestinal mucosa has been determined: Ac-Ser-Ala-Gln-Lys-Ser-Pro-Ala-Glu-Leu-Lys-Ser-Ile-Phe-Glu-Lys-Tyr-Ala-Ala-Lys-Glu-Gly-Asp-Pro-Asn-Gln-Leu-Ser-Lys-Glu-Glu-Leu-Lys-Gln-Leu-Ile-Gln-Ala-Glu-Phe-Pro-Ser-Leu-Leu-Lys-Gly-Pro-Arg-Thr-Leu-Asp-Asp-Leu-Phe-Gln-Glu-Leu-Asp-Lys-Asn-Gly-Asn-Gly-Glu-Val-Ser-Phe-Glu-Glu-Phe-Gln-Val-Leu-Val-Lys-Lys-Ile-Ser-Gln-OH. The N-terminal octapeptide sequence was determined by mass spectrometry analysis by Morris and Dell. The first 45 residues of bovine CaBP differ only in six positions from the corresponding sequence of the porcine protein, except that the sequence starts in position two of the porcine sequence. The mammalian intestinal CaBP's belong to the troponin-C superfamily on the basis of an analysis by Barker and Dayhoff.

Mass spectrometry analysis, amino acid sequence and biological activity of venom components from the Brazilian scorpion Opisthacanthus cayaporum

Toxicon ◽  
2008 ◽  
Vol 51 (8) ◽  
pp. 1499-1508 ◽  
Author(s):  
Elisabeth F. Schwartz ◽  
Thalita S. Camargos ◽  
Fernando Z. Zamudio ◽  
Luciano P. Silva ◽  
Carlos Bloch ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

A new member of the troponin C superfamily: Comparison of the primary structures of rat oncomodulin and rat parvalbumin

1983 ◽  
Vol 3 (11) ◽  
pp. 1071-1075 ◽  
Author(s):  
J. P. Mac Manus ◽  
D. C. Watson ◽  
M. Yaguchi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Isoelectric Point ◽  
Base Pair ◽  
Calcium Binding ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Single Base ◽  
Binding Domains ◽  
Single Base Pair

When the amino-acid sequence of the 108-residue, rat tumour calcium-binding protein, oncomodulin, was aligned with that of rat muscle parvalbumin, 55 homologous positions were found, with an additional 33 single base-pair substitutions. This extensive homology, with virtual identity of the calcium-binding domains, signalled oncomodulin to be a member of the troponin C superfamily. The presence of Cys-18 and Phe-66 in oncomodulin, plus its isoelectric point of 3.9) suggest that this tumour protein is a 8-parva Jbumin, rather than a muscle α-parvalbumin.

scholarly journals Amino acid sequence of vitamin D-dependent calcium-binding protein from bovine cerebellum

FEBS Letters ◽  
1986 ◽  
Vol 201 (1) ◽  
pp. 41-45 ◽  
Author(s):  
Takashi Takagi ◽  
Masanobu Nojiri ◽  
Kazuhiko Konishi ◽  
Kei Maruyama ◽  
Yoshiaki Nonomura
Keyword(s):  
Vitamin D ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein
Sign in / Sign up

Export Citation Format

Share Document