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大肠杆菌HB101(pEAP31)释放青霉素酶,同时Kil肽释放外膜成分。

Release of penicillinase by Escherichia coli HB101 (pEAP31) accompanying the simultaneous release of outer-membrane components by Kil peptide.

作者信息

Aono R

机构信息

Institute of Physical and Chemical Research, Saitama, Japan.

出版信息

Biochem J. 1989 Oct 1;263(1):65-71. doi: 10.1042/bj2630065.

Abstract

The plasmid pEAP31 contains an alkaliphilic-Bacillus penicillinase gene and a colicin E1 kil gene. Escherichia coli HB101 carrying pEAP31 grown at high temperature released outer-membrane proteins, lipopolysaccharide and phosphatidylethanolamine into the culture medium. Concurrently, penicillinase that had accumulated in the periplasm of the organism was released from the cells. Phospholipase A1-A2 in the outer membrane was not activated in the organism. The results suggest that the release of accumulated periplasmic penicillinase from the producer cells was caused by partial disruption of the outer membrane mediated by the Kil peptide.

摘要

质粒pEAP31含有嗜碱芽孢杆菌青霉素酶基因和大肠杆菌素E1 kil基因。携带pEAP31的大肠杆菌HB101在高温下生长时,会将外膜蛋白、脂多糖和磷脂酰乙醇胺释放到培养基中。同时,积聚在该生物体周质中的青霉素酶也从细胞中释放出来。外膜中的磷脂酶A1 - A2在该生物体中未被激活。结果表明,积累在周质中的青霉素酶从产生菌细胞中的释放是由Kil肽介导的外膜部分破坏所导致的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44b4/1133391/fb107e140996/biochemj00198-0074-a.jpg

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