High-molecular-weight protein aggregates of calf and cow lens: Spectroscopic evaluation
Tài liệu tham khảo
Andley, 1982, Spectroscopic investigations of bovine lens crystallins. 2. Fluorescent probes for polar-apolar nature and sulfhydryl group accessibility, Biochemistry, 21, 1853, 10.1021/bi00537a023
Andley, 1984, Changes in tertiary structure of calf-lens α-crystallin by near-u.v. irradiation: role of hydrogen peroxide, Photochem. Photobiol., 40, 343, 10.1111/j.1751-1097.1984.tb04597.x
Bose, 1986, Sensitizer-induced conformation changes in lens crystallin—II. Photodynamic action of riboflavin on bovine α-crystallin, Photochem. Photobiol., 43, 525, 10.1111/j.1751-1097.1986.tb09530.x
Chakrabarti, 1987, Light-induced conformational changes of lens proteins: photochemistry and photophysics of the process, 712, 154
Chiou, 1979, Isolation and physical characterization of bovine lens crystallins, Int. J. Pept. Protein Res., 13, 409, 10.1111/j.1399-3011.1979.tb01900.x
Coopman, 1984, Physicochemical studies on bovine eye lens proteins. II. Comparative physical study of low-molecular-weight α-crystallins from calf lens cortical and nuclear fiber cells, Exp. Eye Res., 38, 463, 10.1016/0014-4835(84)90124-6
Harding, 1976, Structural proteins of the mammalian lens: a review with emphasis on changes in development, aging and cataract, Exp. Eye Res., 22, 1, 10.1016/0014-4835(76)90033-6
Horwitz, 1976, Some properties of the low molecular weight α-crystallin from normal human lens: comparison with bovine lens, Exp. Eye Res., 23, 471, 10.1016/0014-4835(76)90156-1
Horwitz, 1977, Conformation of gamma-crystallins of the calf lens: effect of temperature and denaturing agents, Exp. Eye Res., 25, 199, 10.1016/0014-4835(77)90132-4
Jedziniak, 1973, On the presence and mechanism of formation of heavy molecular weight aggregates in human normal and cataractous lenses, Exp. Eye Res., 15, 185, 10.1016/0014-4835(73)90118-8
Laemmli, 1970, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature (London), 227, 680, 10.1038/227680a0
Lawson, 1981, The solubility of bovine lens crystallins, J. Biol. Chem., 256, 6523, 10.1016/S0021-9258(19)69017-4
Liang, 1982, Spectroscopic investigations of bovine lens crystallins. 1. Circular dichroism and intrinsic fluorescence, Biochemistry, 21, 1847, 10.1021/bi00537a022
Liem-The, 1975, Further characterization of HM-crystallin in rabbit lens, Exp. Eye Res., 20, 307, 10.1016/0014-4835(75)90113-X
Mandal, 1986, Sensitizer-induced conformational changes in lens crystallin—I. Photodynamic action of methylene blue and N-formylkynurenine on bovine γ-crystallin, Photochem. Photobiol., 43, 515, 10.1111/j.1751-1097.1986.tb09529.x
Mandal, 1987, Differences in photoinduced structural changes of γ-crystallins: spectroscopic and HPLC studies, Invest. Ophthalmol. Vis. Sci., 28, 387
Mandal, 1987, Structure and stability of γ-crystallins: denaturation and proteolysis behavior, J. Biol. Chem., 17, 8096, 10.1016/S0021-9258(18)47533-3
Ozaki, 1983, Raman spectroscopic study of age-related structural changes in the lens proteins of an intact mouse lens, Biochemistry, 22, 6254, 10.1021/bi00295a033
Parker, 1968
Roy, 1976, High molecular weight protein from human lenses, Exp. Eye Res., 22, 273, 10.1016/0014-4835(76)90055-5
Sabés, 1987, Detection of charge-perturbation of tryptophan residues by fourth-derivative spectrophotometry, Photochem. Photobiol., 45, 657, 10.1111/j.1751-1097.1987.tb07394.x
Sigelman, 1974, Quantitative biomicroscopy of lens light back scatter: changes in aging and opacification, Arch. Ophthalmol., 92, 437, 10.1001/archopht.1974.01010010449016
Spector, 1982, Aging of the lens and cataract formation, 27