Characteristics of asparagine-linked sugar chains of sphingolipid activator protein 1 purified from normal human liver and GM1 gangliosidosis (type 1) liver

Biochemistry ◽  
1990 ◽  
Vol 29 (12) ◽  
pp. 3030-3039 ◽  
Author(s):  
Katsuko Yamashita ◽  
Koji Inui ◽  
Kazuhide Totani ◽  
Naohisa Kochibe ◽  
Masumi Furukawa ◽  
...  
1987 ◽  
Vol 248 (3) ◽  
pp. 937-941 ◽  
Author(s):  
P G Board ◽  
K Pierce

A plasmid, termed pTacGST2, which contains the complete coding sequence of a GST2 (glutathione S-transferase 2) subunit and permits the expression of the protein in Escherichia coli was constructed. The expressed protein had the same subunit Mr as the enzyme from normal human liver and retained its catalytic function with both GST and glutathione peroxidase activity. Antiserum raised against the bacterially synthesized protein cross-reacted with all the basic GST isoenzymes in human liver. The electrophoretic mobility in agarose of the bacterially expressed isoenzyme suggested that its pI is identical with that of the cationic isoenzyme from human liver previously termed GST2 type 1. The available evidence suggests that the three common cationic isoenzymes found in human liver are the products of two very similar gene loci.


2009 ◽  
Vol 18 (10) ◽  
pp. 1417-1422 ◽  
Author(s):  
Katalin Dezső ◽  
Sándor Paku ◽  
Veronika Papp ◽  
Eszter Turányi ◽  
Peter Nagy

2018 ◽  
Vol 120 (5) ◽  
pp. 7907-7917 ◽  
Author(s):  
Paolo Fais ◽  
Martina Leopizzi ◽  
Valeria Di Maio ◽  
Lucia Longo ◽  
Carlo Della Rocca ◽  
...  

10.4081/965 ◽  
2009 ◽  
Vol 49 (4) ◽  
pp. 371 ◽  
Author(s):  
D Fanni ◽  
L Pilloni ◽  
S Orrù ◽  
P Coni

1980 ◽  
Vol 58 (6) ◽  
pp. 494-498 ◽  
Author(s):  
M. Pagé ◽  
J. Lagueux ◽  
C. Gauthier

We describe a method for the purification of normal human liver ferritin by ultrafiltration, gel filtration on Sephacryl S-300, and affinity chromatography on DEAE-Affi Gel Blue. The purity of the ferritin obtained was verified by immunoelectrophoresis, Ouchterlony immunodiffusion, polyacrylamide gel electrophoresis, and electrofocusing. This rapid method yields 32% of the original ferritin.


Nature ◽  
1974 ◽  
Vol 251 (5476) ◽  
pp. 655-656 ◽  
Author(s):  
KURT SCHUMACHER ◽  
GISEALA MAERKER-ALZER ◽  
URSEL WEHMER

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