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1
Purification of D-alanine carboxypeptidase from Escherichia coli B on a penicillin-Sepharose column.利用青霉素-琼脂糖凝胶柱从大肠杆菌B中纯化D-丙氨酸羧肽酶
Biochem J. 1975 Apr;147(1):131-7. doi: 10.1042/bj1470131.
2
Isolation of D-alanine carboxypeptidase by affinity chromatography.通过亲和色谱法分离D-丙氨酸羧肽酶。
Methods Enzymol. 1974;34:398-401. doi: 10.1016/s0076-6879(74)34045-1.
3
D-alanine carboxypeptidase activity of Micrococcus lysodeikticus released into the protoplasting medium.溶菌微球菌释放到原生质体形成培养基中的D-丙氨酸羧肽酶活性。
Eur J Biochem. 1975 Jun 16;55(1):291-7. doi: 10.1111/j.1432-1033.1975.tb02162.x.
4
Purification of a nocardicin A-sensitive LD-carboxypeptidase from Escherichia coli by affinity chromatography.通过亲和层析法从大肠杆菌中纯化对诺卡菌素A敏感的LD-羧肽酶。
J Bacteriol. 1992 Jan;174(2):441-6. doi: 10.1128/jb.174.2.441-446.1992.
5
Purification to homogeneity and properties of two D-alanine carboxypeptidases I From Escherichia coli.来自大肠杆菌的两种D-丙氨酸羧肽酶I的纯化至均一性及性质
J Biol Chem. 1976 Jan 25;251(2):414-23.
6
Purification and characterization of an arginine-specific carboxypeptidase from Mycoplasma salivarium.唾液支原体精氨酸特异性羧肽酶的纯化与特性分析
J Bacteriol. 1988 Apr;170(4):1795-9. doi: 10.1128/jb.170.4.1795-1799.1988.
7
Purification of a human urinary carboxypeptidase (kininase) distinct from carboxypeptidases A, B, or N.一种不同于羧肽酶A、B或N的人尿羧肽酶（激肽酶）的纯化。
Anal Biochem. 1984 Aug 1;140(2):520-31. doi: 10.1016/0003-2697(84)90203-3.
8
Purification of carboxypeptidase A using Sepharose 4B-bound 3-phenylpropionate.
J Biochem. 1977 May;81(5):1285-91.
9
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.
10
Simultaneous deletion of D-alanine carboxypeptidase IB-C and penicillin-binding component IV in a mutant of Escherichia coli K12.在大肠杆菌K12突变体中同时缺失D-丙氨酸羧肽酶IB-C和青霉素结合成分IV。
Proc Natl Acad Sci U S A. 1977 Jul;74(7):2980-4. doi: 10.1073/pnas.74.7.2980.

引用本文的文献

1
Knockout of the two ldh genes has a major impact on peptidoglycan precursor synthesis in Lactobacillus plantarum.敲除两个乳酸脱氢酶基因对植物乳杆菌中肽聚糖前体的合成有重大影响。
J Bacteriol. 1996 Sep;178(18):5431-7. doi: 10.1128/jb.178.18.5431-5437.1996.
2
Murein biosynthesis in ether permeabilized Escherichia coli starting from early peptidoglycan precursors.从早期肽聚糖前体开始，在经乙醚通透处理的大肠杆菌中进行胞壁质生物合成。
Arch Microbiol. 1981 Dec;130(4):301-6. doi: 10.1007/BF00425944.
3
Inhibition of peptidoglycan biosynthesis in gram-positive bacteria by LY146032.LY146032对革兰氏阳性菌肽聚糖生物合成的抑制作用。
Antimicrob Agents Chemother. 1987 Jul;31(7):1093-9. doi: 10.1128/AAC.31.7.1093.

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
DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.圆盘电泳。II. 方法及其在人血清蛋白中的应用。
Ann N Y Acad Sci. 1964 Dec 28;121:404-27. doi: 10.1111/j.1749-6632.1964.tb14213.x.
3
The enzymatic addition of D-alanyl-D-alanine to a uridine nucleotide-peptide.将D-丙氨酰-D-丙氨酸酶促添加到尿苷核苷酸-肽上。
J Biol Chem. 1962 May;237:1601-4.
4
A modified colorimetric method for the estimation of N-acetylamino sugars.一种用于估算N-乙酰氨基糖的改良比色法。
J Biol Chem. 1955 Dec;217(2):959-66.
5
Isolation and study of the chemical structure of a disaccharide from Micrococcus lysodeikticus cell walls.
J Biol Chem. 1966 Jan 10;241(1):223-30.
6
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定分子量的可靠性。
J Biol Chem. 1969 Aug 25;244(16):4406-12.
7
On the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin.关于青霉素、万古霉素和瑞斯托菌素对白链霉菌G D-羧肽酶的作用机制。
Biochemistry. 1970 Jul 21;9(15):2971-5. doi: 10.1021/bi00817a006.
8
Substrate requirements of the Streptomyces albus G DD carboxypeptidase.白色链霉菌G型DD羧肽酶的底物需求
Biochemistry. 1970 Jul 21;9(15):2961-70. doi: 10.1021/bi00817a005.
9
Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11.来自链霉菌菌株R39和K11的青霉素敏感型DD-羧肽酶
Biochemistry. 1972 Mar 28;11(7):1290-8. doi: 10.1021/bi00757a027.
10
Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61.来自链霉菌菌株R 61的青霉素敏感型DD-羧肽酶
Biochemistry. 1971 May 25;10(11):2163-70. doi: 10.1021/bi00787a032.

利用青霉素-琼脂糖凝胶柱从大肠杆菌B中纯化D-丙氨酸羧肽酶

Purification of D-alanine carboxypeptidase from Escherichia coli B on a penicillin-Sepharose column.

作者信息

Gorecki M, Bar-Eli A, Burstein Y, Patchornik A, Chain E B

出版信息

Biochem J. 1975 Apr;147(1):131-7. doi: 10.1042/bj1470131.

DOI:10.1042/bj1470131
PMID:1098657
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1165382/
Abstract
  1. A soluble D-alanine carboxypeptidase from Escherichia coli strain B was purified on a p-aminobenzylpenicillin-Sepharose column. This one-step chromatography followed by an (NH4)2SO4 precipitation yielded an enzyme purified 1200-fold and some of its properties are reported. 2. The pure D-alanine carboxypeptidase was devoid of D-alanine carboxypeptidase II activity and migrated as a single protein band on analytical disc gel electrophoresis. 3. Triton X-100 in the purification procedure is an absolute requirement for obtaining a stable enzyme. 4. The enzymic activity of D-alanine carboxypeptidase was greatly affected in solution of high salt concentrations and varied somewhat with the nature of the cation tested.
摘要
  1. 从大肠杆菌B菌株中纯化出一种可溶性D-丙氨酸羧肽酶，该酶在对氨基苄青霉素-琼脂糖柱上进行纯化。经这一步层析，再进行硫酸铵沉淀，得到了纯化1200倍的酶，并报道了其一些性质。2. 纯化的D-丙氨酸羧肽酶没有D-丙氨酸羧肽酶II活性，在分析盘状凝胶电泳上迁移为单一蛋白条带。3. 纯化过程中的吐温X-100是获得稳定酶的绝对必要条件。4. D-丙氨酸羧肽酶的酶活性在高盐浓度溶液中受到极大影响，并且随所测试阳离子的性质略有变化。