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PMID: 3417675 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The orientation of halorhodopsin in the cell membrane of halobacteria.

The Journal of biological chemistry ·Vol. 263 ·No. 27 ·1988-09-25 ·Pages 13623-5

May KM, Jay FA, Oesterhelt D

Abstract

The orientation of the light-driven chloride pump, halorhodopsin, in the membrane was determined using antibodies directed against a synthetic peptide which represents the C-terminal segment of the protein. Antibodies against this decapeptide did not bind to right-side-out cell vesicles. Partial inversion by sonication or lysis under low salt conditions exposed this COOH-terminal antigenic site. Antibody binding was removed by preincubation with the decapeptide. The COOH terminus of the molecule is therefore located on the cytoplasmic surface of the membrane.

MeSH Terms
Amino Acid Sequence Bacteriorhodopsins/analysis Cell Membrane/analysis Cytoplasm/analysis Enzyme-Linked Immunosorbent Assay Halobacterium/analysis,ultrastructure Halorhodopsins Molecular Sequence Data Protein Conformation
Chemicals
Halorhodopsins Bacteriorhodopsins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
May K M
Max-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.
Jay F A
Oesterhelt D
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1988-09-25
Pages
13623-5
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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