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

研究成果: Article査読

50 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)993-999
ページ数7
ジャーナルBiochemical and Biophysical Research Communications
128
2
DOI
出版ステータスPublished - 1985 4月 30

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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