Inhibition of alpha-crystallin aggregation by gamma-crystallin.
نویسندگان
چکیده
منابع مشابه
Alpha-crystallin.
Alpha A and alpha B-crystallins are a major protein component of the mammalian eye lens. Being a member of the small heat-shock protein family they possess chaperone-like function. The alpha-crystallins and especially alpha B is also found outside the lens having an extensive tissue distribution. Alpha B-crystallin is found to be over-expressed in many neurological diseases, and mutations in al...
متن کاملPreferential interaction of alpha crystallin with denatured forms of gamma crystallin.
PURPOSE To characterize the possible interaction of alpha crystallin with partially denatured forms of gamma crystallin. METHODS Gamma crystallin was denatured in the presence of guanidine hydrochloride, then dialyzed in the presence or absence of alpha crystallin. The high-molecular-weight complex formed in the presence of alpha was characterized by gel filtration chromatography, electron mi...
متن کاملHuman alpha-crystallin. I. The isolation and characterization of newly synthesized alpha-crystallin.
Studies of the incorporation of 14C amino acids into human lens proteins demonstrate that an alpha-crystallin fraction takes up more than six times as much radioactivity as any other lens protein. Based on analyses with a calibrated Bio-Gel A-1.5 m column, a molecular weight of 4.9 x 10(5) +/- 5 per cent was obtained for this protein while sedimentation equilibrium analyses indicated a weight a...
متن کاملMechanism of Suppression of Protein Aggregation by α-Crystallin
This review summarizes experimental data illuminating the mechanism of suppression of heat-induced protein aggregation by alpha-crystallin, one of the small heat shock proteins. The dynamic light scattering data show that the initial stage of thermal aggregation of proteins is the formation of the initial aggregates involving hundreds of molecules of the denatured protein. Further sticking of t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)34050-5