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[Studies on human chorionic gonadotropin (HCG)-binding protein from Pseudomonas maltophilia by ligand blotting assay].

Authors
  • Li, X
  • Chen, M
  • Lan, T
Type
Published Article
Journal
Hua xi yi ke da xue xue bao = Journal of West China University of Medical Sciences = Huaxi yike daxue xuebao / [bian ji zhe, Hua xi yi ke da xue xue bao bian wei hui]
Publication Date
Sep 01, 1992
Volume
23
Issue
4
Pages
377–380
Identifiers
PMID: 1304539
Source
Medline
License
Unknown

Abstract

A ligand blotting technique was developed to study the HCG-binding protein from Pseudomonas maltophilia after size separation by SDS-polyacrylamide gel electrophoresis under nonreducing conditions. The separated proteins were transferred to a nitrocellulose sheet, which was subsequently incubated with [125I]iodo HCG, and subjected to determination for radioactivity in gamma-counter. A radioactivity peak equivalent to an M(r) 70000 appeared, which was not observed when the hormone incubation was performed in the presence of an excess of unlabeled HCG. The peak also disappeared when the protein samples were treated with reducing agent, which showed that integrity disulfide bonds of the protein was essential for the protein-hormone interaction. In addition, position of the radioactivity peak which was due to the binding of [125I]iodo HCG to western blots of the HCG-binding protein was corresponding to that of the antibodies against the HCG-binding protein recognizing a 70000 protein on the western blots. These results show that the HCG-binding protein from Pseudomonas maltophilia is an M(r) 70000 protein and that the HCG-binding protein contains at least one disulfide bond essential to its binding activity.

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