Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes

• Published in: The Journal of general physiology Vol. 96; no. 3; pp. 631 - 664
• Main Authors: EHRING, G. R, ZAMPIGHI, G, HORWITZ, J, BOK, D, HALL, J. E
• Format: Journal Article
• Language: English
• Published: New York, NY Rockefeller University Press 01.09.1990; The Rockefeller University Press
• Subjects: Animals; Aquaporins; Biological and medical sciences; Cattle; Chromatography, High Pressure Liquid; Electric Conductivity; Eye and associated structures. Visual pathways and centers. Vision; Eye Proteins - chemistry; Eye Proteins - isolation & purification; Eye Proteins - metabolism; Freeze Fracturing; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; In Vitro Techniques; Ion Channels - chemistry; Ion Channels - metabolism; Kinetics; major intrinsic protein; Membrane Glycoproteins; Molecular Structure; Potassium Chloride; Vertebrates: nervous system and sense organs; Electrical properties; Intrinsic protein; HPLC chromatography; Electrophysiology; Ox; Ionic channel; Gap junction; Eye; Visual system; Vertebrata; Mammalia; Plasma membrane; Lens; Artiodactyla; Ungulata

Detergent-solubilized plasma membrane protein of either adult bovine or calf lens and high-performance liquid chromatography-purified major intrinsic protein (MIP) of the lens were reconstituted into unilamellar vesicles and planar lipid bilayers. Freeze-fracture studies showed that the density of i...