Major intrinsic polypeptide of lens membrane. Biochemical and immunological characterization of the major cyanogen bromide fragment

Larry J. Takemoto, Jeff S. Hansen, Bruce J Nicholson, Michael Hunkapiller, Jean Paul Revel, Joseph Horwitz

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

A protein of Mr 26 000 has been shown to be the major component of eye-lens junctions, which are similar but not identical to the gap junctions of liver and other tissues. Cyanogen bromide cleavage of the Mr 26 000 polypeptide from bovine lenses yields a major fragment of Mr 15 000 (fragment 1). However, if the junctions are first treated with trypsin or carboxypeptidase Y, cyanogen bromide treatment yields a fragment of reduced molecular weight. Since protease treatment has been shown to cleave residues almost exclusively from the carboxy-terminal end of the Mr 26 000 polypeptide, it follows that fragment 1 represents the carboxy-terminal half of this molecule, part of which is exposed to proteolytic attack outside the membrane. This latter result is corroborated by the fact that antisera which recognize both the Mr 26 000 polypeptide and fragment 1 fail to do so after preadsorption with intact membranes. In addition, comparative amino acid and partial sequence analyses of the Mr 26 000 polypeptide and fragment 1 indicate that fragment 1 is more hydrophilic in character, suggesting that much of the amino-terminal half of the Mr 26 000 polypeptide is buried within the lipid bilayer.

Original languageEnglish (US)
Pages (from-to)267-274
Number of pages8
JournalBBA - Biomembranes
Volume731
Issue number2
DOIs
StatePublished - Jun 10 1983
Externally publishedYes

Fingerprint

Cyanogen Bromide
Lenses
Membranes
Peptides
Cathepsin A
Crystalline Lens
Lipid bilayers
Gap Junctions
Protein Sequence Analysis
Lipid Bilayers
Liver
Trypsin
Immune Sera
Peptide Hydrolases
Molecular Weight
Molecular weight
Tissue
Amino Acids
Molecules
Proteins

Keywords

  • (Bovine and rat eye)
  • Cyanogen bromide cleavage
  • immunological characterization
  • Lens junction
  • Major intrinsic polypeptide

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Medicine(all)

Cite this

Major intrinsic polypeptide of lens membrane. Biochemical and immunological characterization of the major cyanogen bromide fragment. / Takemoto, Larry J.; Hansen, Jeff S.; Nicholson, Bruce J; Hunkapiller, Michael; Revel, Jean Paul; Horwitz, Joseph.

In: BBA - Biomembranes, Vol. 731, No. 2, 10.06.1983, p. 267-274.

Research output: Contribution to journalArticle

Takemoto, Larry J. ; Hansen, Jeff S. ; Nicholson, Bruce J ; Hunkapiller, Michael ; Revel, Jean Paul ; Horwitz, Joseph. / Major intrinsic polypeptide of lens membrane. Biochemical and immunological characterization of the major cyanogen bromide fragment. In: BBA - Biomembranes. 1983 ; Vol. 731, No. 2. pp. 267-274.
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abstract = "A protein of Mr 26 000 has been shown to be the major component of eye-lens junctions, which are similar but not identical to the gap junctions of liver and other tissues. Cyanogen bromide cleavage of the Mr 26 000 polypeptide from bovine lenses yields a major fragment of Mr 15 000 (fragment 1). However, if the junctions are first treated with trypsin or carboxypeptidase Y, cyanogen bromide treatment yields a fragment of reduced molecular weight. Since protease treatment has been shown to cleave residues almost exclusively from the carboxy-terminal end of the Mr 26 000 polypeptide, it follows that fragment 1 represents the carboxy-terminal half of this molecule, part of which is exposed to proteolytic attack outside the membrane. This latter result is corroborated by the fact that antisera which recognize both the Mr 26 000 polypeptide and fragment 1 fail to do so after preadsorption with intact membranes. In addition, comparative amino acid and partial sequence analyses of the Mr 26 000 polypeptide and fragment 1 indicate that fragment 1 is more hydrophilic in character, suggesting that much of the amino-terminal half of the Mr 26 000 polypeptide is buried within the lipid bilayer.",
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AU - Hansen, Jeff S.

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AU - Hunkapiller, Michael

AU - Revel, Jean Paul

AU - Horwitz, Joseph

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N2 - A protein of Mr 26 000 has been shown to be the major component of eye-lens junctions, which are similar but not identical to the gap junctions of liver and other tissues. Cyanogen bromide cleavage of the Mr 26 000 polypeptide from bovine lenses yields a major fragment of Mr 15 000 (fragment 1). However, if the junctions are first treated with trypsin or carboxypeptidase Y, cyanogen bromide treatment yields a fragment of reduced molecular weight. Since protease treatment has been shown to cleave residues almost exclusively from the carboxy-terminal end of the Mr 26 000 polypeptide, it follows that fragment 1 represents the carboxy-terminal half of this molecule, part of which is exposed to proteolytic attack outside the membrane. This latter result is corroborated by the fact that antisera which recognize both the Mr 26 000 polypeptide and fragment 1 fail to do so after preadsorption with intact membranes. In addition, comparative amino acid and partial sequence analyses of the Mr 26 000 polypeptide and fragment 1 indicate that fragment 1 is more hydrophilic in character, suggesting that much of the amino-terminal half of the Mr 26 000 polypeptide is buried within the lipid bilayer.

AB - A protein of Mr 26 000 has been shown to be the major component of eye-lens junctions, which are similar but not identical to the gap junctions of liver and other tissues. Cyanogen bromide cleavage of the Mr 26 000 polypeptide from bovine lenses yields a major fragment of Mr 15 000 (fragment 1). However, if the junctions are first treated with trypsin or carboxypeptidase Y, cyanogen bromide treatment yields a fragment of reduced molecular weight. Since protease treatment has been shown to cleave residues almost exclusively from the carboxy-terminal end of the Mr 26 000 polypeptide, it follows that fragment 1 represents the carboxy-terminal half of this molecule, part of which is exposed to proteolytic attack outside the membrane. This latter result is corroborated by the fact that antisera which recognize both the Mr 26 000 polypeptide and fragment 1 fail to do so after preadsorption with intact membranes. In addition, comparative amino acid and partial sequence analyses of the Mr 26 000 polypeptide and fragment 1 indicate that fragment 1 is more hydrophilic in character, suggesting that much of the amino-terminal half of the Mr 26 000 polypeptide is buried within the lipid bilayer.

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KW - Major intrinsic polypeptide

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