ANTIBIOTICS AS TOOLS FOR METABOLIC STUDIES .V. EFFECT OF NONACTIN MONACTIN DINACTIN AND TRINACTIN ON OXIDATIVE PHOSPHORYLATION AND ADENOSINE TRIPHOSPHATASE INDUCTION
ANTIBIOTICS AS TOOLS FOR METABOLIC STUDIES .V. EFFECT OF NONACTIN MONACTIN DINACTIN AND TRINACTIN ON OXIDATIVE PHOSPHORYLATION AND ADENOSINE TRIPHOSPHATASE INDUCTION
复制标题
DOI：
10.1021/bi00869a040
复制
发表时间：
1966-01-01
期刊：
影响因子：
2.9
通讯作者：
RUTTER, A
中科院分区：
文献类型：
--
作者：
GRAVEN, SN;LARDY, HA;RUTTER, A
研究了四种同源抗生素，nonactin，monactin，dinactin和trinactin对氧化磷酸化和腺苷三磷酸酶（ATP酶）诱导的影响。Nonactin、monactin、dinactin和trinactin在1 × 10-7浓度下解偶联氧化磷酸化[图片]，在1 × 10-8浓度下部分解偶联[图片]。所有4个同系物诱导ATP水解。Monactin，dinactin和trinactin是比nonactin更有效的ATP酶活性诱导剂。抗生素的作用需要一价阳离子Na+、K+、Rb+或Cs+。在Li+作为阳离子的存在下，没有一个nonactin同系物是活跃的。在低抗生素浓度下（1 × 10-7 [图片]及以下），Na+诱导的ATP酶活性低于K+、Rb+或Cs+。在低单价阳离子浓度（7.5 m[图像]）下，在Rb+存在下观察到最大活性。抗生素是氧化磷酸化的有效解偶联剂和ATP酶活性的诱导剂，其活性可能通过对单价阳离子转运的影响介导。通过ATP酶诱导测定，nonactin同系物的活性与缬氨霉素相当，但活性低于短杆菌肽A-D。nonactin同系物的单价阳离子需求使其活性与缬氨霉素、短杆菌肽和短杆菌肽A-D的活性不同。
Four homologous antibiotics, nonactin, monactin, dinactin, and trinactin, were studied for their effect on oxidative phosphorylation and adenosine triphosphatase (ATPase) induction. Nonactin, monactin, dinactin, and trinactin uncoupled oxidative phosphorylation at a concentration of 1 x 10-7 [image] and partially uncoupled at 1 x 10-8 [image]. All 4 homologs induced ATP hydrolysis. Monactin, dinactin, and trinactin were more potent inducers of ATPase activity than nonactin. A monovalent cation, Na+, K+, Rb+, or Cs+, was required for the action of the antibiotics. None of the nonactin homologs was active in the presence of Li+ as the cation. At low antibiotic concentrations (1 x 10-7 [image] and below), less ATPase activity was induced in the presence of Na+ than in the presence of K+, Rb+, or Cs+. At low monovalent cation concentrations (7.5 m[image]), greatest activity was observed in the presence of Rb+. The antibiotics are potent uncouplers of oxidative phosphorylation and inducers of ATPase activity with their activity possibly mediated through an effect on monovalent cation transport. The nonactin homologs were comparable in activity to valinomycin and less active than gramicidins A-D as measured by ATPase induction. The monovalent cation requirement of the nonactin homologs differentiated their activity from that of valinomycin, tyrocidine, and gramicidins A-D.