beta-Galactosidase from rat epididymal fluid is bound by a recognition site attached to membranes of the epididymis different from the phosphomannosyl receptor.
beta-Galactosidase from rat epididymal fluid is bound by a recognition site attached to membranes of the epididymis different from the phosphomannosyl receptor.
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来自大鼠附睾液的β-半乳糖苷酶与附着在附睾膜上的识别位点结合，该识别位点不同于磷酸甘露糖基受体。
DOI：
10.1016/0006-291x(87)90319-6
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发表时间：
1987
影响因子：
3.1
通讯作者：
F. Bertini
中科院分区：
文献类型：
--
作者：
M. Sosa;L. Mayorga;F. Bertini
为了了解大鼠附睾液中的β-半乳糖苷酶是否与其他分泌性酸性水解酶一样，在其分子中携带标记物，我们研究了该酶与附睾组织细胞膜的结合。的结合，如由磷酸甘露糖受体介导的，是饱和的，不需要钙，具有在nM范围内的Kd，并抑制磷酸酶或偏高碘酸盐处理的酶。然而，果糖6-磷酸衍生物是更有效的竞争性抑制剂比甘露糖6-磷酸。用Triton X-100可提取膜的结合容量，并可将其分散到脂质体中。胰蛋白酶抑制Triton提取物的结合能力，但不影响完整细胞膜对β-半乳糖苷酶的亲和力。结果表明，磷酸化的碳水化合物的酶结合的识别位点的细胞膜不同于磷酸甘露糖受体。
In order to know if the β-galactosidase of the rat epididymal fluid, as other secreted acid hydrolases, carries a marker in its molecule, we studied the binding of this enzyme to cellular membranes of the epididymal tissue. The binding, like that mediated by the phosphomannosyl receptor, was saturable, did not require calcium, had a Kd in the nM range and was inhibited by phosphatase or metaperiodate treatment of the enzyme. However fructose 6-phosphate derivates were more effective competitive inhibitors than mannose 6-phosphate. The binding capacity of the membranes were extractable with Triton X-100 and incorporable into liposomes. Trypsin inhibited the binding capacity of Triton extracts but it did not affect the affinity of intact cellular membranes for β-galactosidase. The results suggest that a phosphorylated carbohydrate of the enzyme is bound by a recognizing site of the cellular membranes different from the phosphomannosyl receptor.
大鼠肝脏中的磷酸甘露糖基酶受体。
DOI：
--
发表时间：
1980
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Fischer,HD;Gonzalez-Noriega,A;Sly,WS;Morré,DJ
通讯作者：
Morré,DJ