title: Column chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and two-dimensional electrophoresis of pig lens crystallins.
abstract: An identical size of porcine and bovine lens crystallins could be demonstrated using gel chromatography, while slight differences were found in their relative concentrations. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis, both types of lens crystallins were found very similar, with the only exception of a slightly lower molecular weight of the porcine beta-h and beta-i subunits. By two-dimensional electrophoresis, 14 out of 19 spots likewise coincided. This great similarity in crystallin subunits between both animals agrees with their phylogenetic proximity, and it is suggested that porcine and bovine lenses may be used in very similar ways for investigation of posttranslational modifications of crystallins.
authors.affiliation: Department of Medicine, University of Santiago, Spain.
authors.forename: P
authors.initials: P
authors.lastname: Vidal
authors.forename: J
authors.initials: J
authors.lastname: Cabezas-Cerrato
mesh_terms: D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003459:Crystallins / Q000032:analysis*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D011499:Protein Processing, Post-Translational / Q000502:physiology; D013552:Swine
chemical_list: D003459:Crystallins