Analysis of the proteins in the rhesus monkey lens.
The proteins of the Rhesus monkey (Macaca mulatta) lens were studied and characterized. In general, there is a similarity of the monkey lens to the human lens particularly in the alpha- and beta-crystallins and the membrane proteins, although the amount of beta 1-crystallin may be greater in the monkey. There is immunological cross-reactivity in the crystallins between monkey and human lenses including the monkey low molecular weight proteins and the human low molecular weight proteins. The monkey lens low molecular weight material showed three differently sized proteins by gel exclusion chromatography. In this respect, the monkey lens proteins are similar to the human. However, the monkey lens low molecular weight proteins differ from the human low molecular weight proteins in charge as well as molecular weight determined by SDS-PAGE. One of the monkey low molecular weight proteins is more prevalent in the nucleus than in the cortex suggesting that this protein may be more important to the embryonic lens that to the adult lens.
D000293:Adolescent; D000368:Aged; D000818:Animals; D002850:Chromatography, Gel; D003459:Crystallins / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D007908:Lens, Crystalline / Q000032:analysis* / Q000378:metabolism; D008253:Macaca mulatta; D008565:Membrane Proteins / Q000032:analysis; D008875:Middle Aged; D008970:Molecular Weight; D012333:RNA, Messenger / Q000302:isolation & purification / Q000378:metabolism
D003459:Crystallins; D008565:Membrane Proteins; D012333:RNA, Messenger