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Comparative Study
. 1991 Jun 28;177(3):1025-32.
doi: 10.1016/0006-291x(91)90641-j.

Cloning and characterization of bovine insulin-like growth factor binding protein-3 (bIGFBP-3)

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Comparative Study

Cloning and characterization of bovine insulin-like growth factor binding protein-3 (bIGFBP-3)

S K Spratt et al. Biochem Biophys Res Commun. .

Abstract

We report for the first time the isolation of a cDNA encoding the complete amino acid sequence for bovine growth hormone-dependent insulin-like growth factor binding protein-3 (bIGFBP-3). The deduced amino acid sequence from the cDNA revealed a mature polypeptide consisting of 264 amino acids and a 27 amino acid putative signal peptide. The amino acid sequence is over 80% homologous with human IGFBP-3 with complete conservation of the 18 cysteine residues and the 3 Asn-linked glycosylation sites. Between the two species there are 44 amino acid substitutions. Northern analysis of the bIGFBP-3 mRNA in bovine tissue revealed a single mRNA species of 1.65 kilobases.

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