Isolation of a biologically active fragment from the carboxy terminus of the fetal rat binding protein for insulin-like growth factors

J F Wang; B Hampton; T Mehlman; W H Burgess; M M Rechler

doi:10.1016/s0006-291x(88)80309-7

Isolation of a biologically active fragment from the carboxy terminus of the fetal rat binding protein for insulin-like growth factors

Biochem Biophys Res Commun. 1988 Dec 15;157(2):718-26. doi: 10.1016/s0006-291x(88)80309-7.

Authors

J F Wang¹, B Hampton, T Mehlman, W H Burgess, M M Rechler

Affiliation

¹ Molecular, Cellular and Nutritional Endocrinology Branch, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20892.

PMID: 2974285
DOI: 10.1016/s0006-291x(88)80309-7

Abstract

We have purified a 14 kDa fragment of the 30 kDa binding protein for insulin-like growth factors (IGFs) from BRL-3A cell conditioned medium. The fragment binds IGF-I and IGF-II with similar specificity to the 30 kDa binding protein, but with lower affinity. It corresponds to the carboxy terminus of the native binding protein (residues 148-270), and is thought to arise by proteolysis. We infer that this region of the native binding protein contains, at least in part, the IGF binding domain.

MeSH terms

Amino Acid Sequence
Animals
Binding, Competitive
Cell Line
Chromatography, High Pressure Liquid
Cross-Linking Reagents
Culture Media
Insulin-Like Growth Factor I / metabolism*
Insulin-Like Growth Factor II / metabolism*
Molecular Sequence Data
Molecular Weight
Peptide Fragments / isolation & purification
Peptide Fragments / metabolism
Rats
Receptor, Insulin / isolation & purification*
Receptor, Insulin / metabolism
Receptors, Somatomedin
Somatomedins / metabolism*
Structure-Activity Relationship

Substances

Cross-Linking Reagents
Culture Media
Peptide Fragments
Receptors, Somatomedin
Somatomedins
Insulin-Like Growth Factor I
Insulin-Like Growth Factor II
Receptor, Insulin