Formation of a bacterial toxin (streptolysin S) by resting cells.

Formation of a bacterial toxin (streptolysin S) by resting cells.
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DOI:
10.1084/jem.90.5.373
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发表时间:
1949-11
影响因子:
15.3
通讯作者:
BERNHEIMER, A W
BERNHEIMER, A W
中科院分区:
医学1区
文献类型:
--
作者:
BERNHEIMER, A W

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在特定条件下制备的水洗球菌与多核苷酸(AF)相互作用,在存在可发酵碳水化合物的情况下形成溶链素S。此外,最大限度的毒素形成需要镁、钾和磷酸盐离子的存在。链溶素S的生产既可以进行厌氧也可以进行好氧,但在后一种条件下,显然只有在系统充分还原的情况下。温度对毒素出现的速度有显著的影响,临界热增量的值约为36000。汞离子、亚砷酸盐、醋酸碘、二硝基苯酚、叠氮化物等酶毒均可抑制溶血素S的形成。链溶素S在静息细胞系统中的发展既不依赖于自溶也不依赖于预先形成的毒素的物理提取,而是依赖于毒素的合成。从静息细胞系统的上清液中,可以分离出每毫克干重含有20,000至30,000单位链溶素S的产物。介绍了有关产品pH稳定性的信息。该产品不含链激酶、透明质酸酶和蛋白酶,但具有明显的去氧核糖核酸酶活性。化学分析和其他发现表明,多核苷酸和碳水化合物大量存在,少量但未确定数量的蛋白质存在。凝乳胰蛋白酶、凝乳胰蛋白酶、木瓜蛋白酶或组织蛋白酶而不是其他各种酶使溶血素S失活,这表明蛋白质是其活性所必需的,但毒素的确切化学成分仍有待确定。
The interaction of washed cocci, prepared under specified conditions, and a polynucleotide (AF) results in the formation of streptolysin S provided a fermentable carbohydrate is present. Maximum toxin formation requires, in addition, the presence of magnesium, potassium, and phosphate ions. Streptolysin S production proceeds anaerobically as well as aerobically but under the latter condition, apparently only if the system is sufficiently reducing. Temperature has a marked effect on the rate of appearance of toxin, the critical thermal increment having a value of approximately 36,000. The formation of streptolysin S is inhibited by mercuric ion, arsenite, iodoacetate, dinitrophenol, azide, and other enzyme poisons. The development of streptolysin S in resting cell systems depends neither upon autolysis nor upon physical extraction of preformed toxin but upon toxin synthesis. From the supernatant fluid of the resting cell system, a product containing 20,000 to 30,000 units of streptolysin S per mg. dry weight can be isolated. Information concerning the pH stability of the product is presented. The product is free of streptokinase, hyaluronidase, and proteinase, but possesses appreciable desoxyribonuclease activity. Chemical analyses and other findings indicate that polynucleotide and carbohydrate are present in major amount, and that a small but undetermined quantity of protein is present. Inactivation of streptolysin S by chymotrypsin, ficin, papain, or cathepsin, and not by a variety of other enzymes, indicates that protein is essential for activity, but the precise chemical composition of the toxin remains to be established.