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Tris discriminates between the different α‐glucosidase activities from extracts of human neutrophils
Author(s) -
Ortiz de Apodaca M. Asunción,
Fernandez E.,
la Fuente G.
Publication year - 1992
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01799633
Subject(s) - maltase , tris , enzyme , biochemistry , kidney , chemistry , alpha glucosidase , biology , endocrinology
Summary In an attempt to detect acid maltase deficiency in neutrophils from patients with type II glycogenosis, without interference from the ‘renal’ α‐glucosidase activity present in these cells, we have evaluated the contribution of the renal component in the total activity measured at pH 4.0 in extracts of human neutrophils. The renal contribution is about 13–25% and renal glucosidase appears to be closely related to the enzyme present on the epithelium of small intestine, which is known to be inhibited by Tris. We have used this compound as a selective inhibitor of the renal component of α‐glucosidase activity measured at pH 4.0 in total extracts of neutrophils. Our results demonstrate that 0.1 mol/L Tris is an inhibitor of the renal α‐glucosidase present in neutrophils and can be used to reduce the interference from this enzyme in assays of acid maltase.