Literature DB >> 728064

On the two electrophoretic forms of the human superoxide dismutase A in the homozygote SOD A1.

N Crosti.   

Abstract

Human superoxide dismutase A of the common phenotype SOD A1 is present in two electrophoretic forms in erythrocytes. These forms are charge isomers, easily permuting one into the other. Oxidation and reduction of the copper, partial or complete saturation of the dimers with copper, and presence of thiol groups on the enzyme do not seem to be involved.

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Year:  1978        PMID： 728064     DOI： 10.1007/bf00484730

Source DB:  PubMed          Journal:  Biochem Genet        ISSN： 0006-2928            Impact factor:   1.890


  13 in total

1.  A ferrocyanide charge-transfer complex of bovine superoxide dismutase. Relevance of the zinc imidazolate bond to the redox properties of the enzyme.

Authors:  L Morpurgo; I Mavelli; L Calabrese; A F Agrò; G Rotilio
Journal:  Biochem Biophys Res Commun       Date:  1976-05-17       Impact factor: 3.575

2.  Labile sulfur in human Superoxide dismutase.

Authors:  L Calabrese; G Federici; W H Bannister; J V Bannister; G Rotilio; A Finazzi-Agrò
Journal:  Eur J Biochem       Date:  1975-08-01

3.  A comparison between the common type and a rare genetic variant of human cupro-zinc superoxide dismutase.

Authors:  S Marklund; G Beckman; T Stigbrand
Journal:  Eur J Biochem       Date:  1976-06-01

4.  Observations on the oxidation-reduction properties of bovine erythrocyte superoxide dismutase.

Authors:  J A Fee; P E DiCorleto
Journal:  Biochemistry       Date:  1973-11-20       Impact factor: 3.162

5.  On the mechanism of superoxide dismutase. Reaction of the bovine enzyme with hydrogen peroxide and ferrocyanide.

Authors:  G Rotilio; L Morpurgo; L Calabrese; B Mondovì
Journal:  Biochim Biophys Acta       Date:  1973-04-12

6.  Studies on the reconstituion of bovine erythrocyte superoxide dismutase. 3. Evidence for a strong interdependence between Cu 2+ and Zn 2+ binding in the expression of the spectroscopic properties of the native protein and for a close proximity of the Zn 2+ and Cu 2+ sites.

Authors:  J A Fee
Journal:  Biochim Biophys Acta       Date:  1973-01-25

7.  Superoxide dismutase isozymes in different human tissues, their genetic control and intracellular localization.

Authors:  G Beckman; E Lundgren; A Tärnvik
Journal:  Hum Hered       Date:  1973-04       Impact factor: 0.444

8.  Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis.

Authors:  J L Hedrick; A J Smith
Journal:  Arch Biochem Biophys       Date:  1968-07       Impact factor: 4.013

9.  The binding of copper ions to copper-free bovine superoxide dismutase. Properties of the protein recombined with increasing amounts of copper ions.

Authors:  A Rigo; M Terenzi; P Viglino; L Calabrese; D Cocco; G Rotilio
Journal:  Biochem J       Date:  1977-01-01       Impact factor: 3.857

10.  The presence of zinc in human cytocuprein and some properties of the apoprotein.

Authors:  R J Carrico; H F Deutsch
Journal:  J Biol Chem       Date:  1970-02-25       Impact factor: 5.157
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  3 in total

1.  Evidence for tissue-specific electromorphs of Cu/Zn SOD unrelated to genetic control.

Authors:  N Crosti; P Sausa
Journal:  Biochem Genet       Date:  1980-08       Impact factor: 1.890

2.  Assay and Electrophoresis of Superoxide Dismutase from Red Spruce (Picea rubens Sarg.), Loblolly Pine (Pinus taeda L.), and Scotch Pine (Pinus sylvestris L.) : A Method for Biomonitoring.

Authors:  N E Tandy; R T Di Giulio; C J Richardson
Journal:  Plant Physiol       Date:  1989-06       Impact factor: 8.340

3.  Two sex-linked loci in the leopard frog, Rana pipiens.

Authors:  D A Wright; C M Richards
Journal:  Genetics       Date:  1983-02       Impact factor: 4.562
  3 in total

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