Major intrinsic polypeptide (MIP26K) from lens membrane: Reconstitution into vesicles and inhibition of channel forming activity by peptide antiserum

M. Gooden, D. Rintoul, M. Takehana, L. Takemoto

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

Bovine and human lens membrane, when reconstituted into lipid vesicles containing oxidized cytochrome C, will mediate the transmembrane passage of ascorbate into the vesicles, where the reduction of cytochrome C is measured spectrophotometrically. This channel forming activity is specifically inhibited by antiserum made against a synthetic octapeptide near the C-terminus of MIP26K. Together, these studies describe a direct and more sensitive assay system for measurement of channel-forming activity of MIP26K, and suggest that the C-terminus of this molecule may be particularly important in the regulation of channel formation.

Original languageEnglish
Pages (from-to)993-999
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume128
Issue number2
DOIs
Publication statusPublished - 1985 Apr 30

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Cytochromes
Lenses
Immune Sera
Membranes
Peptides
Assays
Lipids
Molecules

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Major intrinsic polypeptide (MIP26K) from lens membrane : Reconstitution into vesicles and inhibition of channel forming activity by peptide antiserum. / Gooden, M.; Rintoul, D.; Takehana, M.; Takemoto, L.

In: Biochemical and Biophysical Research Communications, Vol. 128, No. 2, 30.04.1985, p. 993-999.

Research output: Contribution to journalArticle

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