Characterization of γ-glutamyltranspeptidase in the liver of the frog: 1. Comparison to the rat liver enzyme

1994 ◽  
Vol 12 (1) ◽  
pp. 11-19 ◽  
Author(s):  
Susan J. Sulakhe-Hemmings ◽  
Hongmei Xing
Keyword(s):  
Liver Enzyme ◽  
Rat Liver

scholarly journals Characterization of a rat liver Golgi sulphotransferase responsible for the 6-O-sulphation of N-acetylglucosamine residues in β-linkage to mannose: role in assembly of sialyl-galactosyl-N-acetylglucosamine 6-sulphate sequence of N-linked oligosaccharides

1996 ◽  
Vol 319 (1) ◽  
pp. 209-216 ◽  
Author(s):  
Robert G SPIRO ◽  
Yuichiro YASUMOTO ◽  
Vishnu BHOYROO
Keyword(s):  
Liver Enzyme ◽  
Rat Liver ◽  
Nitrous Acid ◽  
Bovine Milk ◽  
Ph Optimum ◽  
Golgi Membranes ◽  
Triton X

Rat liver Golgi membranes were found to contain an enzyme that can transfer sulphate from 3´-phosphoadenosine 5´-phosphosulphate (PAPS) to C-6 of the terminal GlcNAc in β-linkage to mannose and has properties indicating that it is involved in the synthesis of the NeuAcα2-3(6)Galβ1-4GlcNAc(6-SO4) sequences observed in the N-linked carbohydrate units of various glycoproteins. Assays performed with [35S]PAPS (Km 0.67 µM) and GlcNAcβ1-6Manα1-O-Me (GnMaMe) acceptor (Km 0.71 mM) indicated that the sulphotransferase had a pH optimum of approx. 7.0 and is markedly stimulated by Mn2+ ions (maximum approx. 15 mM) and Triton X-100 (0.05-0.1%). Hydrazine/nitrous acid/NaBH4 treatment of the 35S-labelled product yielded radiolabelled 2,5-anhydromannitol(6-SO4). The sulphated GnMaMe product of the GlcNAc-6-O-sulphotransferase could be galactosylated by a rat liver Golgi enzyme that was shown to have the same properties as the UDP-Gal:GlcNAc β-1,4-galactosyltransferase from bovine milk. Competition studies performed with GlcNAc and GlcNAc-6-SO4 furthermore indicated that the same liver enzyme acted on both acceptors to produce Galβ1-4GlcNAc and Galβ1-4GlcNAc(6-SO4) with Km values of 1.04 and 1.68 mM respectively. Because the sulphated N-acetyl-lactosamine could in turn serve as an acceptor for rat liver sialyltransferase, it seems that this enzyme, together with the Golgi galactosyltransferase and the GlcNAc-6-O-sulphotransferase, could act in concert in assembling the NeuAcα2-3(6)Galβ1-4GlcNAc(6-SO4) branches of complex N-linked oligosaccharides.

Purification and characterization of rat liver enzyme catalyzing stereoselective reduction of acetylpyridines

Chirality ◽  
2005 ◽  
Vol 17 (8) ◽  
pp. 494-500 ◽  
Author(s):  
Koji Uwai ◽  
Noboru Konno ◽  
Shigeyuki Kitamura ◽  
Shigeru Ohta ◽  
Mitsuhiro Takeshita
Keyword(s):  
Liver Enzyme ◽  
Rat Liver ◽  
Purification And Characterization ◽  
Stereoselective Reduction

scholarly journals Purification and Characterization of a Rat Liver Enzyme That Hydrolyzes Valaciclovir, the L-Valyl Ester Prodrug of Acyclovir

1995 ◽  
Vol 270 (26) ◽  
pp. 15827-15831 ◽  
Author(s):  
Thimysta C. Burnette ◽  
Joan A. Harrington ◽  
John E. Reardon ◽  
Barbara M. Merrill ◽  
Paulo de Miranda
Keyword(s):  
Liver Enzyme ◽  
Rat Liver ◽  
Purification And Characterization ◽  
Ester Prodrug

scholarly journals Isolation and characterization of a mannan-binding protein from rat liver.

1981 ◽  
Vol 256 (9) ◽  
pp. 4247-4252
Author(s):  
Y. Mizuno ◽  
Y. Kozutsumi ◽  
T. Kawasaki ◽  
I. Yamashina
Keyword(s):  
Rat Liver ◽  
Binding Protein ◽  
Isolation And Characterization
Sign in / Sign up

Export Citation Format

Share Document