title: Structural studies of lens fiber junction protein MP26 by cyanogen bromide cleavage.
abstract: The lens fiber-cell plasma membrane MP26 from chick, bovine, and human lenses yielded identical cyanogen bromide peptide maps, confirming the essential conservation of structure in the junction protein of vertebrate lens fiber cells. Immunoblot analyses of the cyanogen bromide peptide maps of human lens MP26 and of its age-dependent proteolytic product MP22 confirmed that MP22 is a derivative of MP26. The findings in this study are the first consistent with the positioning of the methionine residues in lens MP26 as predicted by its cDNA-derived sequence.
authors: Department of Anatomy and Cell Biology, Wayne State University School of Medicine, Detroit, Michigan 48201.
authors: J
authors: J
authors: Alcala
authors: J
authors: J
authors: Lawniczak
authors: D
authors: D
authors: Putt
authors: H
authors: H
authors: Maisel
mesh_terms: D000818:Animals; D020346:Aquaporins; D002417:Cattle; D002645:Chickens; D003488:Cyanogen Bromide; D005136:Eye Proteins / Q000032:analysis*; D006801:Humans; D007365:Intercellular Junctions / Q000032:analysis*; D007908:Lens, Crystalline / Q000032:analysis*; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000032:analysis*; D010449:Peptide Mapping
chemical_list: D020346:Aquaporins; D005136:Eye Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; C030328:aquaporin 0; D003488:Cyanogen Bromide