Release of sialyltransferases from rat liver Golgi membranes by a cathepsin D-like proteinase: comparison of the release of Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase, Gal beta 1-3(4)GlcNAc alpha 2-3 sialyltransferase and lactosylceramide alpha 2-3 sialyltransferase (SAT-1)

The activities of Gal beta 1-3(4)GlcNAc alpha 2-3 sialyltransferase and SAT-1 were measured in rat liver Golgi in inflammation; both enzymes decreased by about 50%. This compares with increases of about 3-fold for the Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase. All three sialyltransferases were...

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Veröffentlicht in:	Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology Biochemistry & molecular biology, 1995-02, Vol.110 (2), p.445
Hauptverfasser:	Richardson, K, Jamieson, J C
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Carbohydrate Sequence Cathepsin D - antagonists & inhibitors Cathepsin D - metabolism Chemical and Drug Induced Liver Injury - enzymology Golgi Apparatus - enzymology Hydrogen-Ion Concentration Lysosomes - enzymology Molecular Sequence Data Pepstatins - pharmacology Protein Structure, Tertiary Rats Sialyltransferases - metabolism Turpentine - toxicity
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