scholarly journals Purification and Characterization of Chondroitin 4-Sulfotransferase from the Culture Medium of a Rat Chondrosarcoma Cell Line

1999 ◽  
Vol 274 (4) ◽  
pp. 2456-2463 ◽  
Author(s):  
Shinobu Yamauchi ◽  
Yukie Hirahara ◽  
Hiroaki Usui ◽  
Yoshiko Takeda ◽  
Megumi Hoshino ◽  
...  
2003 ◽  
Vol 83 (6) ◽  
pp. 877-887 ◽  
Author(s):  
Rosario Gil-Benso ◽  
Concha Lopez-Gines ◽  
José Antonio López-Guerrero ◽  
Carmen Carda ◽  
Robert C Callaghan ◽  
...  

Human Cell ◽  
2019 ◽  
Vol 32 (2) ◽  
pp. 202-213
Author(s):  
Rieko Oyama ◽  
Fusako Kito ◽  
Mami Takahashi ◽  
Marimu Sakumoto ◽  
Kumiko Shiozawa ◽  
...  

2001 ◽  
Vol 276 (17) ◽  
pp. 13650-13656 ◽  
Author(s):  
Yasuyuki Hirashima ◽  
Hiroshi Kobayashi ◽  
Mika Suzuki ◽  
Yoshiko Tanaka ◽  
Naohiro Kanayama ◽  
...  

1998 ◽  
Vol 432 (6) ◽  
pp. 529-534 ◽  
Author(s):  
T. Chano ◽  
Hidetoshi Okabe ◽  
Yukikazu Saeki ◽  
Michihito Ishizawa ◽  
Keiji Matsumoto ◽  
...  

1987 ◽  
Vol 262 (33) ◽  
pp. 16087-16094
Author(s):  
J C Gorga ◽  
V Horejsí ◽  
D R Johnson ◽  
R Raghupathy ◽  
J L Strominger

1985 ◽  
Vol 260 (24) ◽  
pp. 13261-13267 ◽  
Author(s):  
D E Ingolia ◽  
C Y Yeung ◽  
I F Orengo ◽  
M L Harrison ◽  
E G Frayne ◽  
...  

1992 ◽  
Vol 288 (2) ◽  
pp. 475-482 ◽  
Author(s):  
I Ishii-Karakasa ◽  
H Iwase ◽  
K Hotta ◽  
Y Tanaka ◽  
S Omura

For the purification of a new type of endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242 (endo-GalNAc-ase-S) [Iwase, Ishii, Ishihara, Tanaka, Omura & Hotta (1988) Biochem. Biophys. Res. Commun. 151, 422-428], a method for assaying enzyme activity was established. Using purified pig gastric mucus glycoprotein (PGM) as the substrate, oligosaccharides liberated from PGM were pyridylaminated, and the reducing terminal sugars of oligosaccharides larger than Gal beta 1-3GalNAc were analysed by h.p.1.c. The crude enzyme of endo-GalNAc-ase-S was prepared as an 80% (w/v) ammonium sulphate precipitate from the concentrated culture medium. The enzyme was partially purified by gel chromatofocusing and subsequent DEAE-Toyopearl chromatography. Endo-enzyme activity eluted around pI 4.8 on a gel chromatofocusing column and eluted with 0.19-0.25 M-NaCl on a DEAE-Toyopearl column. In the enzyme fraction obtained, no exo-glycosidases or proteases could be detected. The molecular mass of the enzyme was estimated as 105 kDa by gel filtration, and the optimum pH was 5.5. Endo-GalNAc-ase-S hydrolysed the O-glycosidic linkage between GalNAc and Ser (Thr) in 3H-labelled and unlabelled asialofetuin, liberating both the disaccharide (Gal beta 1-3GalNAc) and the tetrasaccharide [Gal beta 1-3 (Gal beta 1-4GlcNAc beta 1-6)GalNAc]. When endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. (endo-GalNac-ase-A) was incubated with 3H-labelled and unlabelled asialofetuin, only the disaccharide (Gal beta 1-3GalNAc) was liberated.


Author(s):  
Toshiyuki Kunisada ◽  
Masahiro Miyazaki ◽  
Koichiro Mihara ◽  
Chong Gao ◽  
Akira Kawai ◽  
...  

BMC Cancer ◽  
2018 ◽  
Vol 18 (1) ◽  
Author(s):  
Kiyoto Kanbara ◽  
Yoshinori Otsuki ◽  
Masahito Watanabe ◽  
Syunichi Yokoe ◽  
Yoshiaki Mori ◽  
...  

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