About: Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase

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About: Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase Goto Sponge NotDistinct Permalink

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scientific article published on 01 May 1972

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1972 (uk) artículu científicu espublizáu en mayu de 1972 (ast) scientific article published on 01 May 1972 (en) im Mai 1972 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q68641827-D6591C5D-1F61-47DE-9C20-006809633EAB
publication date	1972-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q68641827-33667EBD-B10E-4071-A4C3-444AC680BD23
language of work or name	English
author name string	wds:Q68641827-045A773A-38C5-49DF-8089-3FBF8EFAA025 wds:Q68641827-169EF917-1FB1-4404-BF60-7251FB58CCF6 wds:Q68641827-3A9AE62B-FA8D-47E3-AA7E-708F213790C0 wds:Q68641827-66225D1C-16C6-46AB-A6C0-D6234110C436 wds:Q68641827-A8D89033-B5D7-49F1-98D4-9FB5AEFFC8C5 wds:Q68641827-D1873CF2-95D5-40C8-913B-975E50BFF148
author name string	F Bossa D Barra G Rotilio L Calabrese B Mondovì A F Agrò
rdfs:label	Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase (en) Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase (nl)
skos:prefLabel	Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase (en) Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase (nl)
name	Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase (en) Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase (nl)
title	wds:Q68641827-7D7E8389-D0E6-47C3-B899-08B3C2495E41
title	Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase (en)
page(s)	wds:Q68641827-03832EE2-E45C-4535-915D-4E0B3E3E81FC
page(s)	2182-2187
instance of	wds:Q68641827-565AC483-7FB1-41EE-98C8-3D09D16E2AA8
instance of	scholarly article
main subject	wds:Q68641827-3FEEE1FE-06BC-4678-B958-6097A9EF55CB
main subject	copper
PubMed ID	wds:Q68641827-04BE5249-8510-4500-91CA-735B84FE0220
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4337490
PubMed ID	4337490
published in	wds:Q68641827-43AF3923-85F2-4C30-BB9E-F54ECEC46C80
published in	Biochemistry
issue	wds:Q68641827-14F69039-DE50-42CE-B56A-AE7197D0A4AE
volume	wds:Q68641827-17148E3D-4DBE-4206-AAAB-4ACC098851AF
issue	11
volume	11
DOI	wds:Q68641827-2A225F4F-DB6A-4EAC-9D3A-92D4395AA153
DOI	http://dx.doi.org/10.1021/BI00761A027
DOI	10.1021/BI00761A027
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68641827
is cites work of	Structural and functional studies of monomeric mutant of Cu-Zn superoxide dismutase without Arg 143 Free radicals in cell biology Role of hepatic lysosomes in the degradation of metallothionein Cobalt Bovine Superoxide Dismutase. Reactivity of the Cobalt Chromophore in the Copper-Containing and in the Copper-Free Enzyme Antioxidative factors in milk. A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase Modification of cysteine 111 in Cu/Zn superoxide dismutase results in altered spectroscopic and biophysical properties. How effective are antioxidant supplements in obesity and diabetes? Hydroperoxide anion, HO2−, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit Role of the electrostatic loop charged residues in Cu,Zn superoxide dismutase Superoxide dismutase and hydrogen peroxide cause rapid nitric oxide breakdown, peroxynitrite production and subsequent cell death Mutation of Lys-120 and Lys-134 drastically reduces the catalytic rate of Cu,Zn superoxide dismutase The induction of metallothionein in rat liver by zinc injection and restriction of food intake The binding of copper ions to copper-free bovine superoxide dismutase. Properties of the protein recombined with increasing amounts of copper ions Labile Sulfur in Human Superoxide Dismutase A study of the electron paramagnetic resonance properties of single monoclinic crystals of bovine superoxide dismutase Superoxide Dismutases: Studies of Structure and Mechanism Molar absorptivity and A1 cm1% values for proteins at selected wavelengths of the ultraviolet and visible regions. XI pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase The binding of copper ions to copper-free bovine superoxide dismutase. Copper distribution in protein samples recombined with less than stoicheiometric copper ion/protein ratios A new look at a time-worn system: oxidation of CuZn-SOD by H2O2. Preparation of selectively metal-free and metal-substituted derivatives by reaction of Cu-Zn superoxide dismutase with diethyldithiocarbamate The superoxide dismutase activity of human erythrocuprein Singlet molecular oxygen in biological systems: non-quenching of singlet oxygen-mediated chemiluminescence by superoxide dismutase. Bis[cyclo(histidylhistidine)]copper(II) complex that mimicks the active center of superoxide dismutase has its catalytic activity The binding of copper ions to copper-free bovine superoxide dismutase. Kinetic aspects Competitive inhibition of Cu, Zn superoxide dismutase by monovalent anions An efficient method for purification of cuprozinc superoxide dismutase from bovine erythrocytes Identification of the residues responsible for the alkaline inhibition of Cu,Zn superoxide dismutase: a site-directed mutagenesis approach The behavior of holo- and apo-forms of bovine superoxide dismutase at low pH A nuclear magnetic relaxation study of Co(II) bovine superoxide dismutase. Evidence that the Co(II) site is exchange-coupled to the copper and not accessible to the solvent Enzyme activity of superoxide dismutase protomers A cupro-zinc protein with superoxide dismutase activity from horse liver. Isolation and properties Effect of Cu,Zn superoxide dismutase on cholesterol metabolism in human hepatocarcinoma (HepG2) cells. Studies of metal-binding properties of Cu,Zn superoxide dismutase by isothermal titration calorimetry. A two-photon ratiometric fluorescence probe for cupric ions in live cells and tissues Reversible uncoupling of the copper and cobalt spin systems in cobalt bovine superoxide dismutase at low pH
is cites work of	wds:Q47863711-301C6430-A84A-4C38-B1CC-539CF40D440F wds:Q44339594-09E2624C-C905-4E7C-9B19-28FD48261A74 wds:Q72067116-F0978481-96B0-4C55-8EF9-4044DA9D02F7 wds:Q30412281-DAAB0770-CD40-447C-B598-8399FF6BBBFC wds:Q37229078-3CCB22E1-B4CE-4792-BACE-A6E3E8A1EBF4 wds:Q39097237-0E3C8A49-24D4-4F27-BA2D-787D1C043ED0 wds:Q42247904-5B040ED1-635A-41FA-9257-2AA214AC7B6F wds:Q40934723-7F5F8513-5509-4796-8932-9B915F770ED5 wds:Q47859009-832A2992-9746-465E-95E8-D09F42375684 wds:Q72716811-7F2979F8-0586-4EAC-ADFC-A0BC054B6D5D wds:Q28087696-C79679BA-0634-478F-9B72-2A6489853679 wds:Q44595350-692DA654-9C9E-4F41-A7AA-D7C9D812F25C wds:Q41052262-249A5838-F5DE-427E-89C7-D338073660D8 wds:Q72796400-0E53FF14-43FE-4D61-BC17-B6D3A602B8B4

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