Title
Micromethod determination of N-acetyl-<tex>$\alpha$</tex>-d-glucosaminidase in human-leukocytes and study of some of its characteristics
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences. Pharmacy
Faculty of Medicine and Health Sciences
Publication type
article
Publication
Oxford ,
Subject
Chemistry
Biology
Source (journal)
The international journal of biochemistry. - Oxford, 1970 - 1994
Volume/pages
25(1993) :2 , p. 209-212
ISSN
0020-711X
ISI
A1993KL92000007
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
1. A very easy fluorescent micromethod is described to measure leukocyte N-acetyl-alpha-D-glucosaminidase in human leukocytes. The method presents the following advantages: possibility to measure low activity due to prolonged linearity, very moderate consumption of substrate, use of total homogenate without the need for protein removal by precipitation after the enzyme reaction, and minimal handling after the addition of the stopping reagent. 2. A number of enzyme characteristics as linearity (up to 16 hr), pH optimum (4), thermoresistance at different temperatures (up to 24 hr at room temperature) and at different pH values (no differences between 3-8) and solubilization by digitonine and Triton X-100 were deter-mined. The characteristics (acid pH optimum, binding to Concanavaline A and stability for prolonged time at 0 and 23-degrees-C) are in agreement with the known properties of most lyosomal enzymes. 3. The specific activity of the enzyme is very low and an unexplained low latency (about 30%) was observed.
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