Quiroga S, Caputto R
Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Argentina.
J Neurochem. 1988 Jun;50(6):1695-700. doi: 10.1111/j.1471-4159.1988.tb02465.x.
An inhibitor of the UDP-N-acetylgalactosamine:GM3, N-acetylgalactosaminyltransferase (EC 2.4.1.92) has been purified close to 100-fold from chicken blood serum. The method of purification includes heating, dialysis, passage through a column of DEAE-Sephadex, filtration through Amicon XM 100, and passage through Sepharose 6B. The molecular weight determined by Sepharose 6B was 200,000, but on sodium dodecyl sulfate-polyacrylamide gel electrophoresis it appears as if the compound dissociated into components of 68,000. The inhibitor was not active on other glycosyl transferases and lost its inhibitory activity following treatment with pronase and trypsin. alpha-Chymotrypsin did not affect the inhibitor. An antibody to this inhibitor was prepared which decreased its inhibitory capability and precipitated with it in a radial double immunodiffusion experiment.
一种UDP-N-乙酰半乳糖胺：GM3 N-乙酰半乳糖胺基转移酶（EC 2.4.1.92）抑制剂已从鸡血清中纯化至近100倍。纯化方法包括加热、透析、通过DEAE-葡聚糖柱、通过Amicon XM 100过滤以及通过琼脂糖6B。通过琼脂糖6B测定的分子量为200,000，但在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上，该化合物似乎解离成68,000的组分。该抑制剂对其他糖基转移酶无活性，在用链霉蛋白酶和胰蛋白酶处理后失去其抑制活性。α-胰凝乳蛋白酶不影响该抑制剂。制备了针对该抑制剂的抗体，该抗体降低了其抑制能力，并在放射状双向免疫扩散实验中与其沉淀。
