Investigation of the alpha-galactosidase deficiency in Fabry's disease using antibodies against the purified enzyme.
Investigation of the alpha-galactosidase deficiency in Fabry's disease using antibodies against the purified enzyme.
复制标题
使用针对纯化酶的抗体研究法布里病中的 α-半乳糖苷酶缺乏症。
DOI：
10.1111/j.1432-1033.1974.tb03600.x
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发表时间：
1974
期刊：
影响因子：
--
通讯作者：
P. Borst
中科院分区：
文献类型：
--
作者：
P. Rietra;J. Molenaar;M. Hamers;J. Tager;P. Borst
1. α-Galactosidase A, the enzyme deficient in Fabry's disease, was purified from normal human urine. The final preparation hydrolysed about 50 μmol p-nitrophenyl-α-galactoside per h per mg protein at 37 °C. An antiserum against this enzyme was raised in rabbits. Preincubation of preparations of normal kidney and urine with the antiserum, followed by centrifugation, led to a marked reduction of the α-galactosidase activity of the preparations.
2. There was no influence of the antiserum on the residual α-galactosidase activity in Fabry kidney or urine, or on an α-galactosidase B preparation from normal urine.
3. Pretreatment of the antiserum with urine or kidney preparations from a Fabry patient did not result in detectable loss of antibodies reacting with α-galactosidase A, as shown by the unimpaired ability of the antiserum to diminish α-galactosidase activity in normal kidney and urine. Furthermore, double immunodiffusion of the pretreated antiserum with a partially purified α-galactosidase preparation, showed that antibodies not absorbable by the Fabry material were still present in the antiserum.
4. Incubation of normal urinary α-galactosidase with antiserum, followed by centrifugation and enzyme assay in the supernatant, led to the same reduction of α-galactosidase activity, regardless of whether a Fabry urine or kidney preparation was simultaneously present or not.
5. It is concluded that no detectable cross-reacting material was present in this case of Fabry's disease.
