The amino acid sequence of porcine intestinal calcium-binding protein
- 31 May 1979
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 57 (6) , 737-748
- https://doi.org/10.1139/o79-092
Abstract
The complete amino acid sequence of the calcium-binding protein (CaBP) from pig intestinal mucosa was 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 spectrometric analysis. The 1st 45 residues of bovine CaBP differ only in 6 positions from the corresponding sequence of the porcine protein, except that the sequence starts in position 2 of the porcine sequence. The mammalian intestinal CaBP belong to the troponin-C superfamily.This publication has 3 references indexed in Scilit:
- Identical precursors for serum transferrin and egg white conalbumin.Journal of Biological Chemistry, 1978
- Ovalbumin: a secreted protein without a transient hydrophobic leader sequence.Proceedings of the National Academy of Sciences, 1978
- [51] Guanidination of proteinsPublished by Elsevier ,1972