Milson D W, Rose F A, Dodgson K S
Biochem J. 1972 Jun;128(2):331-6. doi: 10.1042/bj1280331.
Conditions based on previous assays with potassium p-acetylphenyl sulphate have been established for the specific assay of arylsulphatase C in rat tissues. The enzyme has optimum activity with 40mm substrate at pH8.0 in the presence of 0.1m-phosphate buffer. Under these conditions arylsulphatase C can be assayed without interference from the other arylsulphatase enzymes present and is useful as a marker for the endoplasmic reticulum in cell-fractionation studies.
基于先前对硫酸对乙酰苯酯的测定,已建立了大鼠组织中芳基硫酸酯酶C特异性测定的条件。该酶在pH8.0的0.1m磷酸盐缓冲液存在下,以40mm底物具有最佳活性。在这些条件下,可以测定芳基硫酸酯酶C,而不受其他存在的芳基硫酸酯酶的干扰,并且在细胞分级分离研究中可用作内质网的标志物。