Ando Y
J Bacteriol. 1979 Oct;140(1):59-64. doi: 10.1128/jb.140.1.59-64.1979.
The exudate of fully germinated spores of Clostridium perfringens was found to contain a large amount of a spore lytic enzyme which acted directly on alkali-treated spores of the organism to cause germination. Although no detectable amount of the enzyme was found in dormant spores during germination in a KCl medium, the enzyme was produced rapidly and released into the medium. The optimal conditions for enzyme activity were pH 6.0 and 45 degrees C. Maximum activity occurred in the presence of various univalent cations at a concentration of 50 mM. The enzyme was readily inactivated by several sulfhydryl reagents. A strong reducing condition was generated in the ionic germination of the spores, a minimum Eh level of -350 mV being reached 30 min after initiation of germination. Furthermore, adenosine triphosphate-dependent pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) was identified in both dorman and germinated spores. The relationship between the release of active enzyme and the generation of reducing conditions during germination is discussed.
已发现产气荚膜梭菌完全萌发的孢子的渗出物含有大量的孢子溶解酶，该酶直接作用于经碱处理的该生物体的孢子以使其萌发。尽管在KCl培养基中萌发期间在休眠孢子中未发现可检测量的该酶，但该酶迅速产生并释放到培养基中。酶活性的最佳条件是pH 6.0和45℃。在各种单价阳离子浓度为50 mM的情况下出现最大活性。该酶很容易被几种巯基试剂灭活。在孢子的离子萌发过程中产生了强烈的还原条件，萌发开始后30分钟达到最低Eh水平-350 mV。此外，在休眠和萌发的孢子中均鉴定出依赖三磷酸腺苷的丙酮酸：铁氧化还原蛋白氧化还原酶（EC 1.2.7.1）。讨论了萌发过程中活性酶的释放与还原条件的产生之间的关系。
