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  The use of octyl beta-D-glucoside as detergent for hog kidney brush border membrane

Lin, J.-T., Riedel, S., & Kinne, R. (1979). The use of octyl beta-D-glucoside as detergent for hog kidney brush border membrane. Biochimica et Biophysica Acta-Biomembranes, 557(1), 179-187. doi:10.1016/0005-2736(79)90100-7.

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 Creators:
Lin, Jiann-Trzuo1, Author           
Riedel, Silke1, Author           
Kinne, Rolf1, Author           
Affiliations:
1Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              

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Free keywords: Octyl glucoside; Detergent solubilization; (Brush border membrane)
 Abstract: Octyl β-d-glucoside was synthetized from α-acetobromoglucose with an improved method yielding a very pure product with a sharp melting point (108–109°C) and free of intermediate products as judged by IR and NMR spectra. The yield of the synthesis is 66% when referred to α-acetobromoglucose. The potency of this compound as a detergent on hog kidney brush border membranes was compared to the action of Triton X-100. Octyl glucoside preferentially extracts aminopeptidase M and γ-glutamyltrans-peptidase in a concentration-dependent manner. The more deeply imbedded membrane enzyme, alkaline phosphatase, was relatively resistent to the action of octyl glucoside. In contrast, Triton X-100 extracted all membrane proteins to about the same extent. Additionally it was found that octyl glucoside can be removed from membrane extracts by Biobead SM 2. The capacity of the beads is about 170 mg detergent/g of dry Biobead SM 2. Thus octyl glucoside seems to be a useful tool for solubilization and purification of brush border membranes proteins.

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Language(s): eng - English
 Dates: 1979-02-262003-01-281979-10-19
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0005-2736(79)90100-7
PMID: 549635
 Degree: -

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Title: Biochimica et Biophysica Acta-Biomembranes
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 557 (1) Sequence Number: - Start / End Page: 179 - 187 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702