title: [1H-NMR study on protein of normal and galactose cataractous rat whole lenses].
abstract: The non-invasive method of 1H-nuclear magnetic resonance (1H-NMR) spectroscopy was applied to rat whole lens. The alterations of aging and experimentally induced cataract on protein structures in rat lenses were examined by comparing high resolution 1H-NMR spectra. 1H-NMR measurements were carried out using the water suppression method and resolution enhancement method. The 1H-NMR spectra of normal lens showed narrow resonance lines of lactate and broad ones of aliphatic amino acid residues of lens protein. There was no remarkable change in the spectral pattern of normal lenses within one week. There was also no effect of aging on the spectral pattern of normal lenses. On the other hand the lines due to the aliphatic amino acid residues of the galactose cataractous lens protein were narrower than those of normal lens. This finding suggests that the increase of mobilities of the residues caused by galactose cataract is reflected by the spectral pattern.
authors.affiliation: Department of Ophthalmology, Kyoto Prefectural University of Medicine, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Kaizuka
mesh_terms: D000818:Animals; D002386:Cataract / Q000139:chemically induced / Q000378:metabolism*; D003459:Crystallins / Q000378:metabolism*; D005690:Galactose; D006859:Hydrogen; D007908:Lens, Crystalline / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains
chemical_list: D003459:Crystallins; D006859:Hydrogen; D005690:Galactose