论文部分内容阅读
Purpose: To analyze the change of water-soluble-protein (WSP), urea-soluble-protein (USP) and membrane intrinsic protein (MIP) in human senile catarct. Methods:The water-soluble-fractions (WSF) were prepared basically according to the method of Kibbelear, et al. But in this study, 5mmol/L B-mercaptoethanol was added to the buffer solution. The urea-soluble-fractions (USF) were prepared basically according to the method of Kibbelear, et al. Lens fiber cell membranes were purified basically according to the method of Russell, et al. SDS-PAGE were performed according to the procedure of Laemmili, et al. using resolving gel 13% and 3% stacking gel.Results: The WSP was fractionated into HM+α-, β1-3- and γ-crystallin components. In nuclear cataractous lenses HM + α- and B-crystallin increase, while r-crystallin decrease. The USP from clear lenses contains mainly αβ chains of 22KD, whereas in cataractous lenses, especially in nuclear cataractous lenses, the relative amount of the 28- and 23KD polypeptide
Methods: To analyze the change of water-soluble-protein (WSP), urea-soluble-protein (USP) and membrane intrinsic protein (MIP) in human senile catarct. Methods: According to the method of Kibbelear, et al. But in this study, 5 mmol / L B-mercaptoethanol was added to the buffer solution. The urea-soluble-fractions (USF) were prepared basically according to the method of Kibbelear, Lens fiber cell membranes were purified completely according to the method of Russell, et al. SDS-PAGE were performed according to the procedure of Laemmili, et al. Using resolving gel 13% and 3% stacking gel. Results: The WSP was fractionated into HM + α-, β1-3- and γ-crystallin components. In nuclear cataracty lenses HM + α- and B-crystallin increase, while r-crystallin decrease. The USP from primary lenses containing mainly αβ chains of 22KD, while in cataractous lenses, especially in nuclear cataractous lenses, the relative amount of the 28- an d 23KD polypeptide