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Phase separation of rat intestinal brush border membrane proteins using Triton X-114

Authors
  • Tiruppathi, Chinnaswamy
  • Alpers, David H.
  • Seetharam, Bellur
Type
Published Article
Journal
Analytical Biochemistry
Publication Date
Jan 01, 1986
Volume
153
Issue
2
Pages
330–335
Identifiers
DOI: 10.1016/0003-2697(86)90100-4
Source
Elsevier
Keywords
License
Unknown

Abstract

Rat intestinal microvillus membrane contains at least 24 polypeptides, of which 18 can be solubilized using Triton X-114 at 4°C. Upon phase separation at 32°C, 11 proteins separated nearly completely into the detergent-rich phase, while 9 proteins were found exclusively in the aqueous phase. Enzymes which were uniquely included in the detergent phase were alkaline phosphatase, leucine aminopeptidase, γ-glutamyl transpeptidase, and Ca 2+Mg 2+ ATPase. The proteins which were excluded from the detergent phase and found exclusively in the aqueous phase included the disaccharidases (glucoamylase, sucrase-isomaltase, trehalase, lactase) and the ileal receptor for the intrinsic factor-cobalamin complex. Integral membrane proteins can thus be separated during solubilization into two groups prior to further purification or characterization.

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