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培养哺乳动物细胞的糖鞘脂β-半乳糖苷酶。来自小鼠细胞系LMTK和人类莱施-奈恩成纤维细胞的酶的特性

Glycosphinoglipid beta-galactosidases of cultured mammalian cells. Characterization of the enzymes from mouse cell line lmtk and human Lesch-Nyhan fibroblasts.

作者信息

Rushton A R, Dawson G

出版信息

Biochim Biophys Acta. 1975 Apr 18;388(1):92-105.

PMID:236034
Abstract

Evidence is presented for the existence of three distinct mammalian glycosphingolipid beta-galactosidase responsible for the hydrolysis of galactosylceramide, lactosylceramide and GM1 gangliside, respectively. Activity toward the (L-3-H)galactose-labeled substrates differed with respect to pH optimum, thermostability, effect of NaCl and inhibition by glycosides and related glycosphinglpids. Comparison of these enzymic acitivites in cultured mouse cell line LMTK- and human beta-galactosiddases could probably be detected in future experiments with somatic cell hybrids (formed by the fusion of these two cell strains by specifically inhibiting activity of mouse origin.

摘要

有证据表明存在三种不同的哺乳动物糖鞘脂β-半乳糖苷酶,分别负责水解半乳糖神经酰胺、乳糖神经酰胺和GM1神经节苷脂。对(L-3-H)半乳糖标记底物的活性在最适pH、热稳定性、NaCl的影响以及糖苷和相关糖鞘脂的抑制作用方面存在差异。在培养的小鼠细胞系LMTK-和人β-半乳糖苷酶中比较这些酶活性,在未来用体细胞杂种(通过这两种细胞株融合形成,通过特异性抑制小鼠来源的活性)进行的实验中可能检测到。

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