Isolation of a low molecular mass vasoactive intestinal peptide binding protein

A vasoactive intestinal peptide (VIP) binding protein was purified in active form by detergent solubilization of lung membranes, gel filtration, VIP-Sepharose affinity chromatography, reverse phase high performance liquid chromatography, and anion exchange chromatography. The mass of this protein wa...

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Bibliographic Details
Published in:The Journal of biological chemistry 1991-09, Vol.266 (27), p.18358-18362
Main Authors: BRUGGER, C. H, STALLWOOD, D, PAUL, S
Format: Article
Language:English
Subjects:
Aminoacids, peptides. Hormones. Neuropeptides
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Chromatography, Liquid
Cross-Linking Reagents
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Guinea Pigs
Magnesium - metabolism
Molecular Weight
plasma membranes
Proteins
Receptors, Gastrointestinal Hormone - isolation & purification
Receptors, Vasoactive Intestinal Peptide
Vasoactive Intestinal Peptide - metabolism
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Summary:A vasoactive intestinal peptide (VIP) binding protein was purified in active form by detergent solubilization of lung membranes, gel filtration, VIP-Sepharose affinity chromatography, reverse phase high performance liquid chromatography, and anion exchange chromatography. The mass of this protein was estimated at 18 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 17 kDa by gel filtration. The binding of VIP by this protein was inhibited by Mg2+, covalent cross-linking of [Tyr10-125I]VIP to the protein produced two radioactive bands at 22 and 26 kDa identified by electrophoresis, and the purified protein exhibited saturable and high affinity binding of VIP and the related neuropeptide, rat growth hormone releasing factor.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)55278-9