Document Detail


Purification and some properties of alpha-L-fucosidase isolated from Streptococcus sanguis.
MedLine Citation:
PMID:  281337     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
alpha-L-Fucosidase acting on naturally occurring substrates was highly purified from the growth culture of Streptococcus sanguis ATCC 10557. The molecular weight of the enzyme was approximately 120,000 and the optimal pH was at 5.5. The purified enzyme showed specificity toward the linkage of alpha-(1 leads to 2) fucosides in oligosaccharides and glycoproteins. The enzyme released L-fucose from glycoprotein in human parotid saliva.
Authors:
S Shizukuishi; T Taniguchi; S Shibata; R Nakamura; A Tsunemitsu; Y Uesugi
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of dental research     Volume:  57     ISSN:  0022-0345     ISO Abbreviation:  J. Dent. Res.     Publication Date:    1978 Nov-Dec
Date Detail:
Created Date:  1979-02-21     Completed Date:  1979-02-21     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0354343     Medline TA:  J Dent Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1028-35     Citation Subset:  D; IM    
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MeSH Terms
Descriptor/Qualifier:
Chromatography, Gas
Chromatography, Gel
Chromatography, Ion Exchange
Electrophoresis, Disc
Glycoproteins / metabolism
Isoelectric Focusing
Molecular Weight
Oligosaccharides / metabolism
Salivary Proteins and Peptides / metabolism
Streptococcus sanguis / enzymology*
Substrate Specificity
alpha-L-Fucosidase / isolation & purification*,  metabolism
Chemical
Reg. No./Substance:
0/Glycoproteins; 0/Oligosaccharides; 0/Salivary Proteins and Peptides; EC 3.2.1.51/alpha-L-Fucosidase

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


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