1974
DOI: 10.1093/oxfordjournals.jbchem.a130419
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The Broad Aglycon Specificity of α-L-Fucosidases from Marine Gastropods

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1976
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Cited by 56 publications
(18 citation statements)
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“…The human endo#acetyl-/3-D-glucosaminidase activity found had a similar pH optimum to those described in rat tissues [2,4,5]. Furthermore, the ratios of the two activities (towards GP-IIIA and ASTF) differed in the various tissues of the same individual, indicating the presence of two separate enzyme proteins, as was suggested for the rat [ 5 1.…”
Section: Discussionsupporting
confidence: 55%
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“…The human endo#acetyl-/3-D-glucosaminidase activity found had a similar pH optimum to those described in rat tissues [2,4,5]. Furthermore, the ratios of the two activities (towards GP-IIIA and ASTF) differed in the various tissues of the same individual, indicating the presence of two separate enzyme proteins, as was suggested for the rat [ 5 1.…”
Section: Discussionsupporting
confidence: 55%
“…Endoglucosaminidase activity towards oligomannosidic glycans was reported in rat and pig tissues [2]. This finding was confirmed [4], localizing this type of enzymatic activity in the cytosolic fraction of rat liver and kidney, with an oligomannosidic substrate derived from ovalbumin.…”
Section: Introductionsupporting
confidence: 57%
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“…also showed this type of specificity. On the other hand, the rt-L-fucosidases from mammalian tissues,8 '" 10) abalone 11 ) and a marine gastropod 12 ) readily hydrolyzed p-nitrophenyl rt-L-fucoside and also liberated fucose slowly from mucin, but seemed not to hydrolyze blood group substances.…”
mentioning
confidence: 99%