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Lysosomal enzymes in human platelets
Author(s) -
Leoncini Giuliana,
Balestrero Flavio,
Maresca Mitzi
Publication year - 1985
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.290030207
Subject(s) - enzyme , heat stability , acid phosphatase , platelet , chemistry , biochemistry , substrate (aquarium) , glucuronidase , fucosidase , human blood , biology , glycoprotein , immunology , ecology , materials science , fucose , composite material , physiology
In human freshly prepared platelets the following lysosomal enzymes were studied: α‐mannosidase, α‐fucosidase, β‐galactosidase, β‐glucosidase, β‐glucuronidase, β‐ N ‐acetylglucosaminidase and acid phosphatase. For each of the examined enzymes the conditions providing maximal activity (pH, buffer), kinetic parameters (saturating substrate concentration and K m ) as well as heat stability were established. On the basis of these parameters it is suggested that many of the serum glycohydrolases may be platelet derived.