Erickson R P, Steers E
J Bacteriol. 1970 Apr;102(1):79-84. doi: 10.1128/jb.102.1.79-84.1970.
The enzyme beta-galactosidase was studied in crude extracts of Escherichia coli 3300, E. coli grown on a selenium and sulfur medium, Salmonella typhimurium F-lac, Serratia marcescens F-lac, S. marcescens P-lac, Proteus mirabilis F-lac, P. mirabilis P-lac, Aeromonas formicans, and Streptococcus lactis. The isoenzymes could be demonstrated by an alternative histochemical technique. Different isoenzyme patterns were found to be determined by the beta-galactosidase structural gene and not by the cytoplasm within which the beta-galactosidase was formed. In addition, the beta-galactosidases from strains which form isoenzymes were more stable to heat and urea treatments than the enzyme formed by those organisms which produce reduced amounts of, or no, isoenzyme.
对以下几种菌株的粗提物中的β-半乳糖苷酶进行了研究:大肠杆菌3300、在含硒和硫的培养基上生长的大肠杆菌、鼠伤寒沙门氏菌F-lac、粘质沙雷氏菌F-lac、粘质沙雷氏菌P-lac、奇异变形杆菌F-lac、奇异变形杆菌P-lac、甲酸气单胞菌和乳酸链球菌。可以通过另一种组织化学技术来证明同工酶的存在。发现不同的同工酶模式是由β-半乳糖苷酶结构基因决定的,而不是由β-半乳糖苷酶形成所在的细胞质决定的。此外,与产生少量或不产生同工酶的生物体所形成的酶相比,形成同工酶的菌株中的β-半乳糖苷酶对热和尿素处理更稳定。