期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：1991
卷号：37
期号：4
页码：419-424
DOI：10.3177/jnsv.37.419
出版社：Center for Academic Publications Japan
摘要：Highly purified lysosomes were isolated from the livers of control and pyridoxine-deficient rats. The calculation of the lysosomal protein contents indicated that the livers of both groups of rats contain virtually the same amounts of the lysosomal proteins (12.0 and 13.0mg lysosomal proteins/g liver proteins for the control and pyridoxine-deficient rats, respectively). The immunoblotting of the lysosomal proteins with anti-cytosolic aspartate aminotransferase (cAspAT) showed 46 kDa band, corresponding to the subunit molecular weight of cAspAT, as well as the bands representing degradative intermediates of cAspAT. The relative amounts of the immuno-reactive substances were estimated by scanning the immuno-stained bands and measuring the densitometric tracings. It was found that the lysosomes in the pyridoxine-deficient rat liver contain almost twice as much cAspAT and its degradative intermediates as those in the control rat liver. On the basis of these observations, it was concluded that the increased rate of degradation of cAspAT in the liver of the pyridoxine-deficient rats is brought about by the increased rate of sequestration of cAspAT into lysosomes.
关键词：pyridoxine-deficiency;degradation of cytosolic aspartate aminotransferase;lysosomes;immunoblotting
