兔乳腺乙酰辅酶A羧化酶的纯化及某些性质
Purification and some properties of acetyl-coenzyme A carboxylase from rabbit mammary gland.
作者信息
Manning R, Dils R, Mayer R J
出版信息
Biochem J. 1976 Feb 1;153(2):463-8. doi: 10.1042/bj1530463.
Abstract
- Acetyl-Coa carboxylase from lactating-rabbit mammary gland was purified to homogeneity by the criterion of polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. 2. Use of phosphate buffer throughout the purification gave low recovery of enzyme. Consequently, Tris buffers were used in the extraction and in selected stages of the purification procedure. 3. The purified enzyme had a specific activity of 5.15 +/- 0.3 mumol of bicarbonate incorporated/min per mg of protein (mean +/- S.E.M. of five preparations). This represents a purification of 257 +/- 16-fold and a yield of 4.3 +/- 0.13%. 4. The kinetic parameters of the purified enzyme were similar to those reported for the enzyme from other tissue sources. 5. The enzyme was assayed by a spectrophotometric assay and by a [14C]bicarbonate-fixation assay. Short incubation were used in the radio-chemical assay to avoid substantial loss of [14C]bicarbonate.
摘要
- 通过十二烷基硫酸钠存在下的聚丙烯酰胺凝胶电泳标准，将来自泌乳兔乳腺的乙酰辅酶A羧化酶纯化至同质。2. 在整个纯化过程中使用磷酸盐缓冲液导致酶的回收率较低。因此，在提取和纯化过程的特定阶段使用了Tris缓冲液。3. 纯化后的酶比活性为每毫克蛋白质每分钟掺入5.15±0.3微摩尔碳酸氢盐（五次制备的平均值±标准误）。这代表了257±16倍的纯化和4.3±0.13%的产率。4. 纯化后酶的动力学参数与其他组织来源的该酶报道的参数相似。5. 通过分光光度法测定和[14C]碳酸氢盐固定测定法对该酶进行测定。在放射化学测定中使用短时间孵育以避免[14C]碳酸氢盐的大量损失。
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