title: A sheet-like form of alpha-crystallin.
abstract: Complexes containing alpha-crystallin were isolated from crosslinked lens extract using an affinity column constructed with monoclonal antibodies specific for alpha-crystallin. The affinity-purified protein was compared with alpha-crystallins before and after crosslinking. Electron microscopy revealed sheet-like structures in the cross-linked protein from the lens extract compared with spherical structures for the others. Studies on the amino acid composition, tryptophan microenvironments and the interaction with a monoclonal antibody revealed that the complexes consist almost entirely of alpha-crystallin. These results indicate that under certain conditions, alpha-crystallin subunits can adopt a sheet-like form.
authors.affiliation: National Vision Research Institute, Carlton, Victoria, Australia.
authors.forename: A
authors.initials: A
authors.lastname: Stevens
authors.forename: R
authors.initials: R
authors.lastname: Walsh
authors.forename: R C
authors.initials: RC
authors.lastname: Augusteyn
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000911:Antibodies, Monoclonal; D002417:Cattle; D003432:Cross-Linking Reagents / Q000494:pharmacology; D003459:Crystallins / Q000737:chemistry* / Q000187:drug effects / Q000648:ultrastructure*; D005976:Glutaral / Q000494:pharmacology; D007908:Lens, Crystalline / Q000737:chemistry; D008854:Microscopy, Electron
chemical_list: D000596:Amino Acids; D000911:Antibodies, Monoclonal; D003432:Cross-Linking Reagents; D003459:Crystallins; D005976:Glutaral