作者: C.H. Brugger , D. Stallwood , S. Paul
DOI: 10.1016/S0021-9258(18)55278-9
关键词: Vasoactive intestinal peptide 、 Biology 、 High-performance liquid chromatography 、 Molecular mass 、 Gel electrophoresis 、 Size-exclusion chromatography 、 Protein purification 、 Binding protein 、 Biochemistry 、 Chromatography 、 Affinity chromatography
摘要: 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 and anion exchange chromatography. The mass this estimated at 18 kDa sodium dodecyl sulfate-polyacrylamide electrophoresis 17 filtration. VIP inhibited Mg2+, covalent cross-linking [Tyr10-125I]VIP to the produced two radioactive bands 22 26 identified electrophoresis, exhibited saturable related neuropeptide, rat growth hormone releasing factor.