Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. Extraction in n-octyl-beta-D-glucopyranoside and evidence for a tetrameric structure.-Reference-Cited by-同舟云学术

Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. Extraction in n-octyl-beta-D-glucopyranoside and evidence for a tetrameric structure.

Published:1990-05 Issue:15 Volume:265 Page:8675-8680
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Aerts T,Xia J Z,Slegers H,de Block J,Clauwaert J

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. LENS CRYSTALLINS: THE EVOLUTION AND EXPRESSION OF PROTEINS FOR A HIGHLY SPECIALIZED TISSUE

2. Dilemmas of the structural and biochemical organization of lens membranes during differentiation and aging

3. The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning

4. Conformational properties of the main intrinsic polypeptide (MIP26) isolated from lens plasma membranes

5. High-performance liquid chromatography of the main polypeptide (MP26) of lens fiber plasma membranes solubilized with n -octyl β-D-glucopyranoside

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