Kinetics and activity of arylsulfatase A in leukocytes derived from patients with cerebral palsy
نویسنده
چکیده
– enzymes hydrolyzing sulfate ester bonds in numerous structurally very different sulfated compounds (1). Crystal structure of human arylsulfatase A was determined in 1998 and the catalytic mechanism of ASA was suggested and described in detail (2). Physical and chemical properties of ASA have been extensively studied in biological samples of different species (1–4). Also, the catalytic mechanism of ASA was confirmed by kinetic studies of numerous active site mutants (5, 6). However, only a few reports dealing with ASA kinetics in human disorders with decreased ASA activity have been published (7–10).
منابع مشابه
Kinetics and activity of arylsulfatase A in leukocytes derived from patients with cerebral palsy.
Activity and kinetics of arylsulfatase A (ASA, EC 3.1.6.8) were analyzed in leukocyte homogenates derived from patients suffering from cerebral palsy. Lower ASA activity was found in the patients' leukocytes than in controls, as determined by spectrophotometry using chromogenic substrate p-nitrocatechol sulfate (p-NCS). Kinetic parameters, K(m) and v(max), for leukocyte ASA were determined from...
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