منابع مشابه
Cleavage of β-Crystallins During Maturation of Bovine Lens
Results: The identities of the major crystallins and several additional crystallin species missing portions of their Nterminal extensions were identified in the fetal bovine lens. Besides the previously identified form of βB1 missing 15 residues from its N-terminus, forms of βA3 missing 11 and 22 residues were identified. With aging, the βA3 (-22) species became a major protein in the adult bov...
متن کاملCalcium-induced aggregation of bovine lens alpha crystallins.
The theory of light scattering indicates that aggregation of the crystalline lens proteins can produce opacity. Furthermore, it is known that calcium increase? in the cataractous lens. We have, therefore, investigated the effectiveness of calcium ion in producmg aggregates of the soluble proteins of the bovine lens. The experimental restdts show: (1) CaCU produce's aggregates of the soluble pro...
متن کاملAge-dependent association of γ-crystallins with aged α-crystallins from old bovine lens
PURPOSE Previous theoretical and experimental studies have predicted that the loss of weak protein interactions between alpha- and gamma-crystallins could result in a decrease in the transparent properties of the aging lens. METHODS alpha-Crystallins were prepared from the nucleus of old bovine lens, and gamma-crystallins were prepared from whole fetal bovine lens or from the nucleus of old b...
متن کاملThiolation of the gammaB-crystallins in intact bovine lens exposed to hydrogen peroxide.
Oxidative damage of the lens causes disulfide bonds between cysteinyl residues of lens proteins and thiols such as glutathione and cysteine, which may lead to cataract. The effect of H2O2 oxidation was determined by comparing bovine lenses incubated with and without 30 mM H2O2. The H2O2 treatment decreased the glutathione and increased the protein-glutathione and protein-cysteine disulfides in ...
متن کاملAggregation in Aqueous Solutions of Bovine Lens y-Crystallins: Special Role of ys
RESULTS. All of the y-crystallins studied formed large aggregates (or "megamers") in aqueous solutions. However, each protein differed in the relative rates of formation of megamers. ysCrystallin formed megamers much more slowly than y,,and yIVa-crystallin. In solutions containing mixtures of y,, and ys, and y,Va and ys, ys-crystallin significantly suppressed the aggregation of y,,and yIV:i-cry...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)69017-4