Engels W, Kamps M A
Antonie Van Leeuwenhoek. 1981;47(6):509-24. doi: 10.1007/BF00443238.
A cell-bound staphylocoagulase could be detected in chemostat cultures of Staphylococcus aureus 104 under magnesium-and oxygen-limited growth conditions. A distribution study revealed that 81% of the enzyme was membrane-bound and could be optimally released by Triton X-100. The remaining part was located in the periplasmic space and was released during protoplasting of organism. From inhibition studies with cerulenin, quinacrine, lincomycin an chloramphenicol, it was concluded that the cell-bound form was precursor in the secretion of extracellular staphylocoagulase. The involvement of a lipid intermediate/exoprotein-releasing protease system in the secretion of staphylocoagulase, and of exoproteins in general, is discussed.
在金黄色葡萄球菌104的恒化器培养物中，在镁和氧受限的生长条件下可检测到细胞结合的葡萄球菌凝固酶。分布研究表明，81%的酶与膜结合，并且可以被 Triton X-100 最佳释放。其余部分位于周质空间，并在原生质体形成过程中释放。通过用浅蓝菌素、奎纳克林、林可霉素和氯霉素进行抑制研究得出结论，细胞结合形式是细胞外葡萄球菌凝固酶分泌的前体。讨论了脂质中间体/外蛋白释放蛋白酶系统在葡萄球菌凝固酶以及一般外蛋白分泌中的作用。
