白细胞中类固醇硫酸酯酶的荧光测定：具有芳基硫酸酯酶C活性的两种基因不同的酶的证据。
A fluorimetric assay of steroid sulphatase in leukocytes: evidence for two genetically different enzymes with arylsulphatase C activity.
作者信息
van Diggelen O P, Konstantinidou A E, Bousema M T, Boer M, Bakx T, Jöbsis A C
机构信息
Department of Clinical Genetics, Erasmus University, Rotterdam, The Netherlands.
出版信息
J Inherit Metab Dis. 1989;12(3):273-80. doi: 10.1007/BF01799217.
Arylsulphatase C (ASC) activity in leukocytes and fibroblasts measured with 4-methylumbelliferylsulphate, is caused by at least two genetically different sulphatases. One of these is steroid sulphatase (STS). Depending on the substrate concentration, about 10-50% of the ASC activity in leukocytes can be attributed to sulphatases other than STS. Steroid sulphatase can be measured specifically with 4-methylumbelliferylsulphate as the fraction of total ASC activity which is inhibitable by dehydroepiandrosterone sulphate. Using this assay, the adjusted ASC activity in leukocytes from patients with X-linked ichthyosis was 2% of normal. Obligate heterozygotes showed reduced activity.
用4-甲基伞形酮基硫酸盐测定的白细胞和成纤维细胞中的芳基硫酸酯酶C（ASC）活性，是由至少两种基因不同的硫酸酯酶引起的。其中一种是类固醇硫酸酯酶（STS）。根据底物浓度，白细胞中约10%-50%的ASC活性可归因于STS以外的硫酸酯酶。类固醇硫酸酯酶可以用4-甲基伞形酮基硫酸盐特异性测定，作为总ASC活性中可被硫酸脱氢表雄酮抑制的部分。使用这种测定方法，X连锁鱼鳞病患者白细胞中经调整的ASC活性为正常水平的2%。纯合子携带者的活性降低。
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