Singh R P, Setlow P
J Bacteriol. 1978 Apr;134(1):353-5. doi: 10.1128/jb.134.1.353-355.1978.
A simple two-step procedure for purification of enolase from germinated spores or vegetative cells of Bacillus megaterium is described. The procedure resulted in a 1,200-fold purification with production of homogeneous enzyme in approximately 75% yield; the enzymes from spores and cells seemed identical. The molecular weight of the native enzyme was 335,000, with a subunit molecular weight of 42,000. The enzyme required Mg2+ and was inhibited by ethylenediaminetetraacetic acid and fluoride ions. The Michaelis constants for 2-phosphoglyceric acid and Mg2+ were 7.1 X 10(-4) and 4.7 X 10(-4) M, respectively.
本文描述了一种从巨大芽孢杆菌的萌发孢子或营养细胞中纯化烯醇化酶的简单两步法。该方法实现了1200倍的纯化，产生的均一酶产量约为75%；来自孢子和细胞的酶似乎相同。天然酶的分子量为335,000，亚基分子量为42,000。该酶需要Mg2+，并受到乙二胺四乙酸和氟离子的抑制。2-磷酸甘油酸和Mg2+的米氏常数分别为7.1×10(-4)和4.7×10(-4)M。
