scholarly journals Purification and characterization of an endo-beta-galactosidase produced by Diplococcus pneumoniae.

1976 ◽  
Vol 251 (12) ◽  
pp. 3603-3609 ◽  
Author(s):  
S Takasaki ◽  
A Kobata
Keyword(s):  
Purification And Characterization ◽  
Beta Galactosidase

scholarly journals Purification and characterization of .BETA.-galactosidase from kiwifruit.

1990 ◽  
Vol 37 (4) ◽  
pp. 298-305 ◽  
Author(s):  
Hiroshi OGAWA ◽  
Haruji FUKUMOTO ◽  
Toshihiro YANO ◽  
Kenji YAMAMOTO ◽  
Tatsurokuro TOCHIKURA
Keyword(s):  
Purification And Characterization ◽  
Beta Galactosidase

scholarly journals Binding of human liver hydrolases by immobilized lectins

1979 ◽  
Vol 177 (1) ◽  
pp. 175-180 ◽  
Author(s):  
M B Fiddler ◽  
Y Ben-Yoseph ◽  
H L Nadler
Keyword(s):  
Human Liver ◽  
Similar Data ◽  
Galactosidase Activity ◽  
Purification And Characterization ◽  
Ulex Europaeus ◽  
Glucuronidase Activity ◽  
Beta Galactosidase ◽  
Carbohydrate Specificities ◽  
Ulex Europaeus Lectin I

The binding of 22 human liver hydrolase activities by immobilized lectins of six different carbohydrate specificities, namely alpha-D-mannose (glucose), D-N-acetylglucosamine, D-N-acetylgalactosamine, L-fucose, alpha-D-galactose and beta-D-galactose, were examined. Differences in binding among these enzymes and within specific enzymes were observed. For example, the neutral forms of alpha-mannosidase and beta-xylosidase were bound by the Ulex europaeus lectin I (specific for L-fucose), whereas the acidic forms were not. Bandierea simplicifolia lectin (specific for alpha-galactose) bound 65% of beta-glucuronidase activity; recycling experiments demonstrated complete binding of the enzyme that had been eluted with the competitor D-galactose and no binding of the fraction that was not initially bound. These results suggested the presence of two forms of this enzyme. Similar data were obtained for acidic beta-galactosidase activity. These experiments may provide the basis for the expanded use of immobilized lectins for purification and characterization of hydrolases and other glycoproteins.

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