1978
DOI: 10.1177/00220345780570110501
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Purification and Some Properties of a-L-Fucosidase Isolated from Streptococcus sanguis

Abstract: 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.

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Cited by 6 publications
(3 citation statements)
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“…The assay of ax-fucosidase activity was conducted according to the method of Shizukuishi et al 13 using PSM as the substrate. The liberated fucose was estimated by the method of Bhattacharyya and Aminoff14 using Conway units.…”
Section: Methodsmentioning
confidence: 99%
“…The assay of ax-fucosidase activity was conducted according to the method of Shizukuishi et al 13 using PSM as the substrate. The liberated fucose was estimated by the method of Bhattacharyya and Aminoff14 using Conway units.…”
Section: Methodsmentioning
confidence: 99%
“…The purified enzyme was specific for the linkage of a-( -2) fucosides in oligosaccharides and glycoproteins. 3 It had been reported that all of the mammalian a-L-fucosidase characterized by its action on p-nitrophenyl-a-L-fucoside and 2'-fucosyllactose failed to destroy the serological activities of H-substances.12 In individuals of the appropriate blood-group and secretor type, the serological activities of A, B, H, Lea and Leb were detectable in saliva. The saliva is required to heat in a water bath immediately after collection in order to inactivate enzymes which would otherwise destroy the blood-group specific substances.13 Among several enzymes having such actions, an enzyme that is more limited and specific in its action on H-substances was first obtained from Trichomonas foetus.…”
Section: Discussionmentioning
confidence: 99%
“…3 The reaction mixture contained a substrate (300 nmnoles in regard to bound fucose) and 0.1 units of the purified enzyme in a total volume of 0.6 ml of 0.1 M sodium phosphate-0.05 M citrate buffer, pH 5.5. Incubations were conducted at 37 C for 1 hour, and the reactions were stopped by heating the mixture for 3 minutes at 100 C. An aliquot of 0.5 ml from the reaction mixture was then quantitatively transferred to Conway unit for the determination of fucose released.…”
mentioning
confidence: 99%