Biological activities of isolated tunicamycin and streptovirudin fractions.
Biological activities of isolated tunicamycin and streptovirudin fractions.
复制标题
分离的衣霉素和链病毒卢定组分的生物活性。
DOI：
10.1021/bi00513a039
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Elbein,AD
中科院分区：
文献类型：
--
作者：
Keenan,RW;Hamill,RL;Occolowitz,JL;Elbein,AD
罗伊·W Robert L.约翰·L·哈米尔Occolowitz和Alan D. Elbein摘要：核苷类抗生素衣霉素和链霉病毒素用高效液相色谱法分离成一系列256 nm吸收峰。大多数的链霉病毒素峰从Biosil ODS柱洗脱早于衣霉素，表明它们的疏水性较低。除第一个峰外，其他17个衣霉素峰是长羟焦磷酸-A-乙酰葡糖胺形成的有效促进剂，50%抑制溶解的GlcNAc-1-P转移酶需要约10 ng抗生素/mL。衣霉素作为一种研究糖蛋白功能的工具，已广泛应用于细胞生理学、细胞生物学和生物化学领域。衣霉素（Takatuski等人，1971）和链病毒菌素（Eckardt等，1975）都是链霉菌抗生素，已被证明是具有GlcNAc-天冬酰胺连接的寡糖的那些蛋白质中糖基化的有效抑制剂。因此，这两种抗生素通过特异性抑制多萜醇途径中的第一种酶UDP-GlcNAc-多萜醇-P：GlcNAc-1-P β-酶来阻断多萜醇焦磷酸-GlcNac的形成（Tkacz & Lampen，1975; Struck & Lennarz，1977; Waechter & Harford，1977; Ericson et al.，1977; Lehle &坦纳，1976; Heifetz等人，1979年）。这些抗生素还抑制葡萄糖从UDP-葡萄糖转移到多酸，
Roy W. Keenan,* Robert L. Hamill, John L. Occolowitz, and Alan D. Elbein abstract: The nucleoside antibiotics tunicamycin and streptovirudin were separated by high-performance liquid chromatography into a series of 256-nm-absorbing peaks. Most of the streptovirudin peaks eluted from a Biosil ODS column earlier than those of tunicamycin, indicating that they were less hydrophobic. With the exception of the first peak, 17 other tunicamycin peaks were potent inhibitorsof the formation of dolichylpyrophosphoryl-A-acetylglucosamine with 50% inhibition of the solubilized GlcNAc-1-P transferase requiring about 10 ng of antibiotic per mL. These fractionsTunicamycin has been widely used in cell physiology, cell biology, and biochemistry as a tool to probe the role of car-bohydrates in glycoprotein functions. Tunicamycin (Takatuski et al., 1971) and streptovirudin (Eckardt et al., 1975) are both streptomycete antibiotics that havebeen shown to be potent inhibitors of glycosylation in those proteins that have a GlcNAc-asparagine-linked oligosaccharide. Thus, both an-tibiotics block the formation of dolichylpyrophosphoryl-GlcNac by specifically inhibiting the first enzyme in the dolichol pathway, the UDP-GlcNAc-dolichyl-P: GlcNAc-1-P transf-erase (Tkacz & Lampen, 1975; Struck & Lennarz, 1977; Waechter & Harford, 1977; Ericson et al., 1977; Lehle & Tanner, 1976; Heifetz et al., 1979). These antibiotics also inhibit the transfer of glucose from UDP-glucoseto dolic-