Stockland A E, San Clemente C L
J Bacteriol. 1968 Jan;95(1):74-80. doi: 10.1128/jb.95.1.74-80.1968.
Lactate dehydrogenase (LDH) was studied in phage-propagating strains 29, 3A, 6, 81, and 42D of Staphylococcus aureus selected from the five groups in the International-Blair series. Cells were cultivated in Brain Heart Infusion (Difco) under nearly anaerobic conditions and were harvested near the end of the log phase. LDH activity was maximal at the end of the exponential growth period and was measured spectrophotometrically by reduction of p-nitro-blue tetrazolium, with phenazine methosulfate as a coupling agent. Crude enzyme extracts were prepared both by an acetone extraction technique and by sonic treatment. LDH activity for these enzyme preparations was determined by the colorimetric method mentioned and also by measuring the rate of nicotinamide adenine dinucleotide reduction at 340 mmu. The order of activity observed, by use of both assay methods, was 29 > 81 > 6 > 3A > 42D. LDH forms (possibly isoenzymes) for each of 15 strains, which represent the five phage-propagating groups of the International-Blair series, were separated by acrylamide gel electrophoresis. Five forms were distinguished and arbitrarily numbered on the basis of their rate of migration, no. 5 being the slowest component. No one strain had more than four, nor fewer than two, LDH forms. Form 3 appeared in 13 of the 15 strains and was followed in frequency by no. 2, 1, 4, and 5.
对从国际布莱尔系列的五组中选出的金黄色葡萄球菌噬菌体繁殖菌株29、3A、6、81和42D中的乳酸脱氢酶（LDH）进行了研究。细胞在脑心浸液（Difco）中于近厌氧条件下培养，并在对数期结束时收获。LDH活性在指数生长期结束时最高，通过对硝基蓝四氮唑的还原，以吩嗪硫酸甲酯作为偶联剂，用分光光度法进行测定。粗酶提取物通过丙酮提取技术和超声处理两种方法制备。这些酶制剂的LDH活性通过上述比色法测定，也通过测量340毫微米处烟酰胺腺嘌呤二核苷酸的还原速率来确定。使用两种测定方法观察到的活性顺序为29＞81＞6＞3A＞42D。通过丙烯酰胺凝胶电泳分离了代表国际布莱尔系列五个噬菌体繁殖组的15个菌株中每一个菌株的LDH形式（可能是同工酶）。区分出了五种形式，并根据它们的迁移速率任意编号，5号是最慢的组分。没有一个菌株的LDH形式超过四种或少于两种。3号形式出现在15个菌株中的13个菌株中，其次是2号、1号、4号和5号形式，出现频率依次递减。
