Document Detail


Purification and characterization of alpha-galactosidase from watermelon.
MedLine Citation:
PMID:  3007446     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
An alpha-galactosidase [EC 3.2.1.22] was isolated from the fruit of the watermelon, Citrullus battich. The enzyme was purified by procedures including extraction, ammonium sulfate precipitation, and chromatographies on DEAE-Sephadex, CM-Sephadex and Sephadex G-100. The final preparation was found to be fairly homogeneous on disc and SDS-polyacrylamide gel electrophoresis, and sufficiently free from other glycosidase activities. The molecular weight of the enzyme was estimated to be 45,000 by Sephadex G-100 column chromatography and SDS-polyacrylamide gel electrophoresis. The enzyme was most active at pH 4.5 for natural substrates and at 5.9 for artificial substrates. The enzyme liberates the alpha-galactose units from oligosaccharides of the raffinose series and ceramide trihexoside, and the hemagglutination-inhibiting activities of human ovarian cyst B-glycoprotein and blood group B-type ghosts were abolished by the enzyme.
Authors:
T Itoh; Y Uda; H Nakagawa
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of biochemistry     Volume:  99     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1986 Jan 
Date Detail:
Created Date:  1986-05-15     Completed Date:  1986-05-15     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  243-50     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Chromatography, Gel
Chromatography, Ion Exchange
Female
Galactosidases / isolation & purification*
Glycoproteins / metabolism
Humans
Hydrogen-Ion Concentration
Hydrolysis
Molecular Weight
Ovarian Cysts / metabolism
Plants / enzymology*
Trihexosylceramides / metabolism
alpha-Galactosidase / isolation & purification*,  metabolism
Chemical
Reg. No./Substance:
0/Glycoproteins; 0/Trihexosylceramides; EC 3.2.1.-/Galactosidases; EC 3.2.1.22/alpha-Galactosidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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