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普通变形杆菌P18及其青霉素诱导的稳定L型中的青霉素结合蛋白和羧肽酶/转肽酶活性

Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms.

作者信息

Rousset A, Nguyen-Distèche M, Minck R, Ghuysen J M

出版信息

J Bacteriol. 1982 Dec;152(3):1042-8. doi: 10.1128/jb.152.3.1042-1048.1982.

DOI:10.1128/jb.152.3.1042-1048.1982
PMID:6754695
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC221607/
Abstract

The originally penicillin-induced, wall-less stable L-forms of Proteus vulgaris P18, isolated by Tulasne in 1949 and since then cultured in he absence of penicillin, have kept the ability to synthesize the seven penicillin-binding proteins and the various DD- and LD-peptidase activities found in the parental bacteria and known to be involved in wall peptidoglycan metabolism. The stable L-forms, however, secrete during growth both the highly penicillin-sensitive, DD-carboxy-peptidase-transpeptidase penicillin-binding protein PBP4 (which in normal bacteria is relatively loosely bound to the plasma membrane) and the penicillin-insensitive LD-carboxypeptidase (which in normal bacteria is located in the periplasmic region).

摘要

1949年图拉斯内分离出的普通变形杆菌P18最初由青霉素诱导形成的无壁稳定L型,自那时起在无青霉素的情况下培养,它仍保留合成七种青霉素结合蛋白的能力,以及在亲代细菌中发现的、已知参与细胞壁肽聚糖代谢的各种DD-和LD-肽酶活性。然而,稳定的L型在生长过程中会分泌高度青霉素敏感的DD-羧肽酶-转肽酶青霉素结合蛋白PBP4(在正常细菌中它相对松散地结合在质膜上)和青霉素不敏感的LD-羧肽酶(在正常细菌中位于周质区域)。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13ba/221607/cbc8880379eb/jbacter00253-0089-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13ba/221607/cbc8880379eb/jbacter00253-0089-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13ba/221607/cbc8880379eb/jbacter00253-0089-a.jpg

相似文献

1
Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms.普通变形杆菌P18及其青霉素诱导的稳定L型中的青霉素结合蛋白和羧肽酶/转肽酶活性
J Bacteriol. 1982 Dec;152(3):1042-8. doi: 10.1128/jb.152.3.1042-1048.1982.
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引用本文的文献

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Microb Drug Resist. 2014 Jun;20(3):190-8. doi: 10.1089/mdr.2014.0047. Epub 2014 May 5.
2
LD-carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12.大肠杆菌中的亮氨酸羧肽酶活性。II. 从大肠杆菌K12中分离、纯化及鉴定该酶
Arch Microbiol. 1986 Mar;144(2):181-6. doi: 10.1007/BF00414732.

本文引用的文献

1
Existence of L-forms in common bacteria and their possible importance.常见细菌中L型细菌的存在及其可能的重要性。
Nature. 1949 Nov 19;164(4177):876. doi: 10.1038/164876b0.
2
Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
3
Lysis of frozen and thawed cells of Escherichia coli by lysozyme and their conversion into spheroplasts.用溶菌酶裂解冻融的大肠杆菌细胞并将其转化为原生质体。
J Bacteriol. 1960 May;79(5):697-706. doi: 10.1128/jb.79.5.697-706.1960.
4
[Study of the growth, in liquid media, of a strain of Proteus and its L form].[变形杆菌菌株及其L型在液体培养基中的生长研究]
C R Seances Soc Biol Fil. 1963;157:183-5.
5
Use of pressure cell to prepare cell walls from Mycobacteria.使用压力室从分枝杆菌制备细胞壁。
Proc Soc Exp Biol Med. 1959 Mar;100(3):647-9. doi: 10.3181/00379727-100-24730.
6
[Research on L transformations (dwarf forms) in a Proteus strain in synthetic media].
Ann Inst Pasteur (Paris). 1957 Jan;92(1):138-41.
7
Penicillin-binding proteins in bacteria.细菌中的青霉素结合蛋白
Antimicrob Agents Chemother. 1980 Jul;18(1):148-57. doi: 10.1128/AAC.18.1.148.
8
Purification of two DD-carboxypeptidases/transpeptidases with different penicillin sensitivities from Proteus mirabilis.
Eur J Biochem. 1980 Apr;105(2):361-70. doi: 10.1111/j.1432-1033.1980.tb04509.x.
9
Differentiation of mycoplasmatales from bacterial protoplast L-forms by assay for penicillin binding proteins.
Arch Microbiol. 1980 Oct;127(3):297-9. doi: 10.1007/BF00427207.
10
Cooperation of benzylpenicillin and cefoxitin in bacterial growth inhibition.苄青霉素与头孢西丁在抑制细菌生长方面的协同作用。
Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):365-7.