MULTIPLE FORMS OF LACTATE DEHYDROGENASE IN STAPHYLOCOCCUS AUREUS
MULTIPLE FORMS OF LACTATE DEHYDROGENASE IN STAPHYLOCOCCUS AUREUS
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DOI：
10.1128/jb.100.1.347-353.1969
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发表时间：
1969-01-01
影响因子：
3.2
通讯作者：
SANCLEME.CL
中科院分区：
文献类型：
--
作者：
STOCKLAND, AE;SANCLEME.CL
测定了金黄色葡萄球菌PS-6菌株无细胞提取液中NAD依赖性和非NAD依赖性乳酸脱氢酶(LDH)的活性。对NAD依赖的乳酸脱氢酶的数据表明，乳酸的两种异构体的氧化都是由于ANL-乳酸专一性的LDH和乳酸消旋酶。经丙烯酰胺凝胶电泳后，在粗提物和部分纯化的无细胞提取物中检测到两条显示LDH活性的条带。对于乳酸的两种异构体，快带具有非NAD依赖的LDH活性，而慢带对异构体具有很高的NAD依赖的LDH活性，但仅检测到活性或异构体。以乳酸为底物时，两条带均出现，而以乳酸为底物时，仅形成一条慢带。依赖NAD的乳酸脱氢酶与一种非特异性的四唑还原蛋白明显相关，负责慢带的产生。
Activities for nicotinamide adenine dinucleotide (NAD)-dependent and NAD-independent forms of lactate dehydrogenase (LDH) were measured in cell-free extracts ofStaphylococcus aureusstrain PS 6 for thedandlisomers of lactate. Data obtained for the NAD-dependent lactate dehydrogenases indicate that oxidation of both isomers of lactate is due to both anl-lactate-specific LDH and a lactate racemase. After acrylamide gel electrophoresis, two bands exhibiting LDH activity were detected in crude or in partially purified cell-free extracts. The fast band exhibited LDH activity that was not NAD-dependent for both isomers of lactate, whereas, the slow band had very high NAD-dependent LDH activity for thelisomer but just detectable activity or thedisomer. Both bands appeared whend-lactate was used as the substrate, but only the slow band was formed whenl-lactate was the substrate. NAD-dependent LDH, in apparent association with a nonspecific tetrazolium-reducing protein, is responsible for the production of the slow band.