A non-denaturing gel electrophoresis system for the purification of membrane bound proteins.

A. G. Cavinato, R. M. Macleod, Mahmoud Ahmed

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

A new method is described for the purification of a membrane bound glycoprotein, the kappa opioid receptor from human placental tissue. The method uses preparative slab-gel electrophoresis in the presence of the non-denaturing detergent CHAPS. A linear relationship between log molecular weight and SDS PAGE electrophoretic mobility of known molecular weight markers, in the presence of CHAPS, is observed. Using this method, we were able partially to purify an 3H-etorphine binding glycoprotein, from placental villus tissue, with an apparent molecular weight range of 60-70,000. The iodinated glycoprotein migrates in SDS PAGE with an apparent molecular weight of 63,000. This method may be useful for the isolation of membrane bound proteins, especially when an affinity ligand is not available.

Original languageEnglish (US)
Pages (from-to)205-216
Number of pages12
JournalPreparative Biochemistry
Volume18
Issue number2
StatePublished - 1988
Externally publishedYes

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Electrophoresis
Purification
Membrane Proteins
Molecular Weight
Gels
Molecular weight
Membranes
Glycoproteins
Polyacrylamide Gel Electrophoresis
Proteins
Etorphine
Tissue
Chorionic Villi
Electrophoretic mobility
kappa Opioid Receptor
Membrane Glycoproteins
Detergents
Ligands
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate

ASJC Scopus subject areas

  • Biochemistry
  • Genetics

Cite this

A non-denaturing gel electrophoresis system for the purification of membrane bound proteins. / Cavinato, A. G.; Macleod, R. M.; Ahmed, Mahmoud.

In: Preparative Biochemistry, Vol. 18, No. 2, 1988, p. 205-216.

Research output: Contribution to journalArticle

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