About: Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents

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scientific article published on 01 November 1962

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в листопаді 1962 (uk) im November 1962 veröffentlichter wissenschaftlicher Artikel (de) 1962 թվականի նոյեմբերի 1-ին հրատարակված գիտական հոդված (hy) artículu científicu espublizáu en payares de 1962 (ast) scientific article published on 01 November 1962 (en)
publication date	wds:Q79467891-766D047F-F20F-47FC-8DC0-4F94DDF3B7B7
publication date	1962-11-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q79467891-EAF0A370-4342-444C-9016-E6CD2DB05574
language of work or name	English
author name string	wds:Q79467891-3BDE96DC-E13B-42F2-B985-FA31577A4A2B wds:Q79467891-83103318-632C-4D97-BE53-3EC5C3540A1C
author name string	B L VALLEE D J PLOCKE
rdfs:label	Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents (en) Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents (nl)
skos:prefLabel	Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents (en) Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents (nl)
name	Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents (en) Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents (nl)
title	wds:Q79467891-FE1D6665-2AB2-4C48-8BC9-40E7E8954E78
title	Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents (en)
page(s)	wds:Q79467891-D9C9F760-7906-4E58-9C06-F4188879AD76
page(s)	1039-1043
instance of	wds:Q79467891-2327BF59-E087-43B2-AAC2-8D9580800E72
instance of	scholarly article
main subject	wds:Q79467891-80D256FC-9EC7-4DB1-B94C-8ED11F7E4CBC
main subject	Escherichia coli
PubMed ID	wds:Q79467891-A6487442-44CA-42B0-A7A1-CDC68D01FF3D
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13944069
PubMed ID	13944069
published in	wds:Q79467891-8E8F5905-BAF0-44BB-A3C4-80AC11043E8E
published in	Biochemistry
volume	wds:Q79467891-13105479-FD69-45EA-BC2D-13B1C90CBF2C
volume	1
DOI	wds:Q79467891-7D446739-0F2F-42B0-BC74-81419C351EDD
DOI	http://dx.doi.org/10.1021/BI00912A014
DOI	10.1021/BI00912A014
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q79467891
is cites work of	The enzymic cleavage of the carbon-phosphorus bond: Purification and properties of phosphonatase Phosphoglycolate phosphatase from human red blood cells Characterization of a Monomeric Escherichia coli Alkaline Phosphatase Formed upon a Single Amino Acid Substitution Amino acid substitutions at the subunit interface of dimeric Escherichia coli alkaline phosphatase cause reduced structural stability Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes The inhibition of enzymes by beryllium Alkaline Phosphatase, Solution Structure, and Mechanism 31P NMR of alkaline phosphatase Transient growth inhibition of Escherichia coli K-12 by ion chelators: "in vivo" inhibition of ribonucleic acid synthesis Heat-labile bacterial alkaline phosphatase from a marine Vibrio sp Role of metal ions in Escherichia coli alkaline phosphatase. A study of the metal-water interaction by nuclear relaxation rate measurements on water protons Metal ion-induced conformational changes in Escherichia coli alkaline phosphatase Metalloalkaline phosphatases from Bacillus subtilis: physicochemical and enzymatic properties A substrate-induced conformation change in the reaction of alkaline phosphatase from Escherichia coli Use of site-directed mutagenesis to elucidate the role of arginine-166 in the catalytic mechanism of alkaline phosphatase Phosphorus-31 relaxation rate studies of Mn2+ - alkaline phosphatase 31P NMR studies on phosphate binding to the Zn2+, Co2+and Mn2+forms ofEscherichia colialkaline phosphatase Metal Substitutions and Inhibition of Thermolysin: Spectra of the Cobalt Enzyme Sandwich electrochemical immunoassay for the detection of Staphylococcal enterotoxin B based on immobilized thiolated antibodies Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369-->Asn): a mechanism involving one zinc per active site Redox modulation of a phosphatase from Anacystis nidulans THE METAL ION ACTIVATION OF THE ALKALINE BETA-GLYCEROPHOSPHATASE OF RABBIT SMALL INTESTINE. The specific binding of copper(II) to alkaline phosphatase of E. coli The Specific Binding of Zinc(II) to Alkaline Phosphatase of Escherichia coli Two differentiable classes of metal atoms in alkaline phosphatase of Escherichia coli Cobalt(III), a probe of metal binding sites of Escherichia coli alkaline phosphatase ACID INACTIVATION OF AND INCORPORATION OF PHOSPHATE INTO ALKALINE PHOSPHATASE FROM ESCHERICHIA COLI Effects of zinc and other metal ions on the stability and activity of Escherichia coli alkaline phosphatase The Biosynthesis of Apo- and Metalloalkaline Phosphatases of Escherichia coli Alkaline phosphatase of Escherichia coli. Composition Activation of a Mutationally Altered Form of the Escherichia coli Alkaline Phosphatase by Zinc Studies on the active center of alkaline phosphatase of E. coli Low serum alkaline phosphatase activity in Wilson's disease The inhibition and disposition of intestinal alkaline phosphatase Leucine aminopeptidase (bovine lens). The relative binding of cobalt and zinc to leucine aminopeptidase and the effect of cobalt substitution on specific activity Factors Affecting the Activity and Stability of Alkaline Phosphatase in a Marine Pseudomonad The subunit composition of Escherichia coli alkaline phosphatase in 1 M Tris Calorimetry of alkaline phosphatase. Stability of the monomer and effect of metal ion and phosphate binding on dimer stability Fluorescence properties of terbium-alkaline phosphatase Identification of a Bacterial Energy-Transducing ATPase as a Metallo (Zn2+) Protein. Effect of Chelating Agents and Divalent Metal Ions on ATPase Activity Intestinal alkaline phosphatase and inorganic pyrophosphatase activities in the zinc-deficient rat Staphylococcal Acid Phosphatase: Preliminary Physical and Chemical Characterization of the Loosely Bound Enzyme Reactivation of APO liver alcohol dehydrogenase with lead, mercury and cadmium 81Br and 35Cl nuclear magnetic resonance studies of E. Coli alkaline phosphatase POLYPHOSPHATE INHIBITION OF GROWTH OF PSEUDOMONADS FROM POULTRY MEAT. Investigation of the coppermagnesiumalkaline phosphatase system 113Cd nuclear magnetic resonance (NMR) study of the inhibitory effect of methylvinylether/maleic acid (PVM/MA) copolymer on the alkaline phosphatase of Escherichia coli Mn(II) alkaline phosphatase. Electron spin resonance and 31P nuclear magnetic resonance
is cites work of	wds:Q27624883-D425E880-4720-4849-A221-05535C9FC740 wds:Q44612514-4174E097-B6A2-4902-BA28-C721B963B1A3 wds:Q41862966-A2B5CB08-7345-4CF2-B4A1-3DE3A292F115 wds:Q42922701-507E813C-E6F6-4A5C-A210-63699E01F2ED wds:Q69853503-3CAE8A3B-DE0C-44C4-9E57-73D9D140CA49 wds:Q69863114-0A2BA071-DCB7-465F-B15D-5B4163C45964 wds:Q73914913-ADE57CB7-4375-423E-8BF2-71DC03AD1929 wds:Q36278413-4A05B410-2B9F-4DA7-B8B0-0726F3468C73 wds:Q35068430-0CD780D2-D63F-4F96-B21A-0BDE168CC39F wds:Q36383926-B76CE5A8-609C-4C05-AA46-468B11E4BE9F wds:Q40952553-E1337E78-BA08-493C-98A4-E1AC567C65E9 wds:Q47801201-F0408BBB-3772-49D3-8D2F-5B5F51CD2845

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