High molecular weight aggregate from cataractous and normal human lenses: characterization by antisera to lens crystallins.
High molecular weight and low molecular weight fractions were obtained from total soluble proteins of human cataractous and normal lens nuclei. These fractions were analyzed using a solid phase radioimmunoassay that employed monospecific antisera to alpha, beta and gamma crystallins. Relative to the high molecular weight fraction from normal lens nuclei, the high molecular weight fraction from cataractous lens nuclei showed decreased binding to antisera specific for beta and gamma crystallins. These results demonstrate that the polypeptides of the high molecular weight fraction comprise a special class of polypeptides that have preferentially undergone covalent and/or structural changes during the process of human cataractogenesis.
Kodama
T
T
Division of Biology, Kansas State University, Manhattan 66506.
Wong
R
R
Takemoto
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L
D002386:Cataract / Q000378:metabolism*; D002498:Centrifugation; D002845:Chromatography / Q000379:methods; D003459:Crystallins / Q000378:metabolism*; D006801:Humans; D007106:Immune Sera / Q000276:immunology; D007908:Lens, Crystalline / Q000378:metabolism*; D008970:Molecular Weight; D011863:Radioimmunoassay / Q000379:methods
D003459:Crystallins; D007106:Immune Sera