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抗枯草芽孢杆菌D-丙氨酸羧肽酶的抗体不与其他青霉素结合蛋白发生交叉反应。

Antibody to the D-alanine carboxypeptidase of Bacillus subtilis does not cross-react with other penicillin-binding proteins.

作者信息

Buchanan C E, Hsia J, Strominger J L

出版信息

J Bacteriol. 1977 Sep;131(3):1008-10. doi: 10.1128/jb.131.3.1008-1010.1977.

DOI:10.1128/jb.131.3.1008-1010.1977
PMID:70424
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC235559/
Abstract

The fact that antibody to d-alanine carboxypeptidase of Bacillus subtilis does not cross-react with other penicillin-binding proteins suggests that these proteins are not precursors or multimers of the enzyme.

摘要

枯草芽孢杆菌D-丙氨酸羧肽酶抗体与其他青霉素结合蛋白不发生交叉反应,这一事实表明这些蛋白质不是该酶的前体或多聚体。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0cf1/235559/71d2fc9f247c/jbacter00304-0304-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0cf1/235559/d352e6c5ef7a/jbacter00304-0303-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0cf1/235559/71d2fc9f247c/jbacter00304-0304-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0cf1/235559/d352e6c5ef7a/jbacter00304-0303-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0cf1/235559/71d2fc9f247c/jbacter00304-0304-a.jpg

相似文献

1
Antibody to the D-alanine carboxypeptidase of Bacillus subtilis does not cross-react with other penicillin-binding proteins.抗枯草芽孢杆菌D-丙氨酸羧肽酶的抗体不与其他青霉素结合蛋白发生交叉反应。
J Bacteriol. 1977 Sep;131(3):1008-10. doi: 10.1128/jb.131.3.1008-1010.1977.
2
D-alanine carboxypeptidase and cell wall cross-linking in Bacillus subtilis.枯草芽孢杆菌中的D-丙氨酸羧肽酶与细胞壁交联
J Bacteriol. 1974 Feb;117(2):926-7. doi: 10.1128/jb.117.2.926-927.1974.
3
Sequence of active site peptides from the penicillin-sensitive D-alanine carboxypeptidase of Bacillus subtilis. Mechanism of penicillin action and sequence homology to beta-lactamases.来自枯草芽孢杆菌青霉素敏感型D-丙氨酸羧肽酶的活性位点肽序列。青霉素作用机制及与β-内酰胺酶的序列同源性。
J Biol Chem. 1980 May 10;255(9):3964-76.
4
Inhibition of the Bacillus subtilis membrane-bound D-alanine carboxypeptidase by 6-aminopenicillanic acid covalently coupled to sepharose.通过与琼脂糖共价偶联的6-氨基青霉烷酸对枯草芽孢杆菌膜结合D-丙氨酸羧肽酶的抑制作用。
J Bacteriol. 1974 Feb;117(2):783-5. doi: 10.1128/jb.117.2.783-785.1974.
5
Linear, uncross-linked peptidoglycan secreted by penicillin-treated Bacillus subtilis. Isolation and characterization as a substrate for penicillin-sensitive D-alanine carboxypeptidases.由青霉素处理的枯草芽孢杆菌分泌的线性、未交联肽聚糖。作为青霉素敏感的D-丙氨酸羧肽酶底物的分离与特性鉴定。
J Biol Chem. 1980 Dec 10;255(23):11577-87.
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Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.从枯草芽孢杆菌的D-丙氨酸羧肽酶中分离青霉素结合肽。
Proc Natl Acad Sci U S A. 1977 Mar;74(3):1009-12. doi: 10.1073/pnas.74.3.1009.
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Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.青霉素作用机制:青霉素和底物在两种细菌D-丙氨酸羧肽酶中与同一个活性位点丝氨酸共价结合。
Proc Natl Acad Sci U S A. 1979 Jun;76(6):2730-4. doi: 10.1073/pnas.76.6.2730.
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Binding of (14C)penicillin G to the membrane-bound and the purified D-alanine carboxypeptidases from Bacillus stearothermophilus and Bacillus subtilis and its release.(14C)青霉素G与嗜热脂肪芽孢杆菌和枯草芽孢杆菌的膜结合型及纯化的D-丙氨酸羧肽酶的结合及其释放
J Biol Chem. 1974 Nov 10;249(21):6828-35.
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Utilization of a depsipeptide substrate for trapping acyl-enzyme intermediates of penicillin-sensitive D-alanine carboxypeptidases.利用一种缩肽底物捕获青霉素敏感的D-丙氨酸羧肽酶的酰基-酶中间体。
Proc Natl Acad Sci U S A. 1978 Jan;75(1):84-8. doi: 10.1073/pnas.75.1.84.
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Biosynthesis of the peptidoglycan of bacterial cell walls. XVI. The reversible fixation of radioactive penicillin G to the D-alanine carboxypeptidase of Bacillus subtilis.细菌细胞壁肽聚糖的生物合成。第十六部分。放射性青霉素G与枯草芽孢杆菌D-丙氨酸羧肽酶的可逆结合。
J Biol Chem. 1970 Jul 25;245(14):3660-6.

引用本文的文献

1
High-molecular-weight penicillin-binding proteins from membranes of bacilli.来自芽孢杆菌细胞膜的高分子量青霉素结合蛋白。
J Bacteriol. 1981 Dec;148(3):950-5. doi: 10.1128/jb.148.3.950-955.1981.
2
Mapping of the gene for a major penicillin-binding protein to a genetically conserved region of the Bacillus subtilis chromosome and conservation of the protein among related species of Bacillus.
J Bacteriol. 1991 Mar;173(5):1807-9. doi: 10.1128/jb.173.5.1807-1809.1991.

本文引用的文献

1
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.
2
A slide microtechnique for the analysis of immune precipitates in gel.一种用于分析凝胶中免疫沉淀物的玻片显微技术。
Int Arch Allergy Appl Immunol. 1957;10(6):355-60. doi: 10.1159/000228394.
3
Isolation by covalent affinity chromatography of the penicillin-binding components from membranes of Bacillus subtilis.通过共价亲和层析从枯草芽孢杆菌膜中分离青霉素结合成分。
Proc Natl Acad Sci U S A. 1972 Dec;69(12):3751-5. doi: 10.1073/pnas.69.12.3751.
4
Multiple penicillin-binding components in Bacillus subtilis, Bacillus cereus, Staphylococcus aureus, and Escherichia coli.枯草芽孢杆菌、蜡样芽孢杆菌、金黄色葡萄球菌和大肠杆菌中的多种青霉素结合成分。
J Biol Chem. 1972 Sep 10;247(17):5279-88.
5
Inactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in Bacillus subtilis.青霉素和头孢菌素对D-丙氨酸羧肽酶的失活作用在枯草芽孢杆菌中并不致命。
Proc Natl Acad Sci U S A. 1971 Nov;68(11):2814-7. doi: 10.1073/pnas.68.11.2814.
6
Covalent affinity chromatography of penicillin-binding components from bacterial membranes.
Methods Enzymol. 1974;34:401-5. doi: 10.1016/s0076-6879(74)34046-3.
7
D-alanine carboxypeptidase from Bacillus subtilis membranes. I. Purification and characterization.来自枯草芽孢杆菌膜的D-丙氨酸羧肽酶。I. 纯化与特性鉴定。
J Biol Chem. 1973 Oct 10;248(19):6759-66.
8
Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.参与大肠杆菌K12分裂、伸长和形态形成的不同青霉素结合蛋白。
Proc Natl Acad Sci U S A. 1975 Aug;72(8):2999-3003. doi: 10.1073/pnas.72.8.2999.
9
Altered penicillin-binding components in penicillin-resistant mutants of Bacillus subtilis.枯草芽孢杆菌青霉素抗性突变体中青霉素结合成分的改变。
Proc Natl Acad Sci U S A. 1976 Jun;73(6):1816-20. doi: 10.1073/pnas.73.6.1816.
10
Identification of the major penicillin-binding proteins of Escherichia coli as D-alanine carboxypeptidase IA.鉴定大肠杆菌的主要青霉素结合蛋白为D-丙氨酸羧肽酶IA。
J Bacteriol. 1976 Jul;127(1):660-3. doi: 10.1128/jb.127.1.660-663.1976.