Glycation of MP26 and MP22 in bovine lens membranes.
Alkali treated membranes were isolated from mature bovine lenses and incubated with different sugars for 3 weeks to study the effect of glycation on the lens intrinsic membrane proteins, MP26 and MP22. The obtained results show that a) [1-14C] ascorbic acid (ASA) was able to glycate the intrinsic membrane proteins as rapidly as soluble lens proteins; b) on 15% acrylamide gels in SDS, glucose, fructose, galactose and ribose exhibited low activity for crosslinking membrane proteins; whereas ASA, dehydroascorbate (DHA), diketogulonate (DKG), xylosone and threose, all showed not only the formation of protein multimers, but also highly crosslinked products, which did not enter the spacer gel; c) except glycated MP22, all of the crosslinks of MP26 or MP22, and also the glycated MP26, showed cross reactivity with polyclonal MP26 antibody; d) the extent of crosslinking correlated with an equal loss of lysine and arginine contents by amino acid analysis.
Prabhakaram
M
M
Mason Institute of Ophthalmology, University of Missouri, Columbia 65212.
Ortwerth
B J
BJ
D000818:Animals; D020346:Aquaporins; D002417:Cattle; D005136:Eye Proteins / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D066298:In Vitro Techniques; D007908:Lens, Crystalline / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008566:Membranes / Q000378:metabolism; D009005:Monosaccharides / Q000737:chemistry / Q000378:metabolism
D020346:Aquaporins; D005136:Eye Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009005:Monosaccharides; C030328:aquaporin 0