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Gewählte Publikation:

Billich, S; Wissel, T; Kratzin, H; Hahn, U; Hagenhoff, B; Lezius, AG; Spener, F.
Cloning of a full-length complementary DNA for fatty-acid-binding protein from bovine heart.
Eur J Biochem. 1988; 175(3):549-556 Doi: 10.1111/j.1432-1033.1988.tb14227.x
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Co-Autor*innen der Med Uni Graz
Spener Friedrich
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Abstract:
A full-length cDNA for bovine heart fatty-acid-binding protein (H-FABP) was cloned from a lambda gt11 cDNA library established from bovine heart muscle. The cDNA sequence shows an open reading frame coding for a protein with 133 amino acids. Colinearity with the amino acid sequences of four tryptic peptides was asserted. H-FABP isolated from bovine heart begins with an N-acetylated valine residue, however, as derived from analysis of the tryptic, amino-terminal-blocked peptide and the molecular mass of the peptide obtained via secondary-ion mass spectrometry. The molecular mass of the total protein is 14673 Da. Bovine H-FABP is 89% homologous to rat H-FABP and 97% homologous to the bovine mammary-derived growth-inhibition factor described recently by Böhmer et al. [J. Biol. Chem. 262, 15137-15143 (1987)]. Significant homologies were also found with bovine myelin protein P2 and murine adipocyte protein p422. Secondary-structure predictions were proposed for these proteins, based on computer analysis, which reveal striking similarities.
Find related publications in this database (using NLM MeSH Indexing)
Acetylation -
Amino Acids - analysis
Animals -
Base Sequence -
Carrier Proteins - genetics
Cattle -
Chromatography, High Pressure Liquid -
Cloning, Molecular -
Computers -
DNA - analysis DNA - biosynthesis
Fatty Acid-Binding Proteins -
Molecular Sequence Data -
Myocardium - metabolism
Neoplasm Proteins -
Nerve Tissue Proteins -
Peptides - analysis
Protein Biosynthesis -
Protein Conformation -
RNA, Messenger - analysis
Rats -
Sequence Homology, Nucleic Acid -

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