English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

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 13.0 mg 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.

Effect of Pyridoxine-Deficiency on Degradation of Cytosolic Aspartate Aminotransferase in Rat Liver Lysosomes.