Purification to homogeneity of GD3 synthase and partial purification of GM3 synthase from rat brain.
Purification to homogeneity of GD3 synthase and partial purification of GM3 synthase from rat brain.
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从大鼠脑中纯化 GD3 合酶并部分纯化 GM3 合酶。
DOI：
10.1016/0006-291x(90)91957-t
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发表时间：
1990
影响因子：
3.1
通讯作者：
Yu,RK
中科院分区：
文献类型：
--
作者：
Gu,XB;Gu,TJ;Yu,RK
从Triton X-100大鼠脑提取物中分别纯化了一种cmp -唾液酸：GM3唾液基转移酶（GD3合成酶）和一种cmp -唾液酸：lacer唾液基转移酶（GM3合成酶），纯化率分别为10000倍和3000倍。两种酶经亲和层析纯化后，分别在两个连续的CDP-Sepharose柱上进行NaCl梯度洗脱。GD3合成酶的最终纯化是用含有GM3缓冲液的“GM3酸”-Sepharose柱进行特异性洗脱。十二烷基硫酸钠凝胶电泳显示，GD3合成酶有一条主蛋白条带，表观分子量为55000。
A CMP-sialic acid: GM3 sialyltransferase (GD3 synthase) and a CMP-sialic acid: LacCer sialyltransferas (GM3 synthase) have been purified 10,000- and 3,000-fold, respectively, from the Triton X-100 extract of rat brain. The two enzymes were purified and resolved by affinity chromatography on two successive CDP-Sepharose columns by NaCl gradient elution. Final purification of GD3 synthase was achieved by specific elution from a ‘GM3 acid’-Sepharose column with buffer containing GM3. Sodium dodecylsulfate-gel electrophoresis of GD3 synthase revealed a single major protein band with an apparent molecular weight of 55,000.