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Biochemical aspects of α‐ L ‐fucosidase in hepatocellular carcinoma
Author(s) -
Leray Geneviève,
Deugnier Yves,
Jouanolle AnneMarie,
Lehry Dominique,
Bretagne JeanFrançois,
Campion JeanPlerre,
Brissot Pierre,
Treut André Le
Publication year - 1989
Publication title -
hepatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.488
H-Index - 361
eISSN - 1527-3350
pISSN - 0270-9139
DOI - 10.1002/hep.1840090214
Subject(s) - thermostability , fucosidase , hepatocellular carcinoma , enzyme , neuraminidase , substrate (aquarium) , biochemistry , chemistry , isozyme , specific activity , substrate specificity , biology , microbiology and biotechnology , glycoprotein , cancer research , ecology , fucose
Biochemical characteristics of α‐ L ‐fucosidase (α–L–fu–coside hydrolase, EC 3.2.1.51) were studied in tumorous and nontumorous human hepatocellular carcinoma (n=14). Five parameters were studied: (i) specific activity, (ii) thermostability, (iii) enzyme affinity for an artificial substrate (K m ), (iv) isoenzyme patterns of the glycosi‐dase before and after neuraminidase treatment and (v) pH influence on enzyme activity. The specific activity of α‐ L ‐fucosidase was significantly decreased in tumoral liver when compared to nontumoral liver. The curve of pH activity constantly showed a broad optimum centered near pH 5, whereas two optima were always observed in nontumoral areas. In contrast, there was no modification of the thermostability, the substrate affinity and the isoenzyme patterns of α‐ L ‐fucosidase in hepatocellular carcinoma.