Literature DB >> 3511030

Strain variation in bacteriocuprein superoxide dismutase from symbiotic Photobacterium leiognathi.

P V Dunlap, H M Steinman.   

Abstract

Photobacterium leiognathi ATCC 25521 (the type strain and light-organ symbiont of ponyfish) is one of the few bacteria that produces a copper-zinc superoxide dismutase, termed bacteriocuprein. We enzymologically and immunologically characterized the bacteriocuprein superoxide dismutases in sonicates from the type strain and nine additional strains of P. leiognathi, each isolated from the light organ of a separate ponyfish specimen, representing seven ponyfish species. The results indicate considerable strain variation. (i) The level of bacteriocuprein enzymatic activity varied greatly among strains from different species of ponyfish. In four of the nine strains, activity was low or undetectable, while in five strains it was comparable to that in the type strain. (ii) The bacteriocuprein in one strain had a specific activity much lower than that of the type strain, and in another strain, no bacteriocuprein activity and no cross-reactive polypeptide were detectable. (iii) A new electrophoretic variant, which migrated slower than that of strains from fish captured in Thailand and Japan, was identified in strains from fish captured in the Philippine Islands. (iv) Enzymological and immunological differences were observed in bacteriocupreins of strains from male and female specimens of the same ponyfish species, for the two species in which specimens of both sexes were examined. These observations raise the possibility that specific variations in the bacteriocupreins of P. leiognathi might be characteristic of the species, geographical source, or sex of the ponyfish host. Thus, the data indicate that the possibility of strain variation should be considered when other species are screened for bacteriocupreins.

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Year:  1986        PMID: 3511030      PMCID: PMC214430          DOI: 10.1128/jb.165.2.393-398.1986

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  16 in total

1.  Superoxide dismutase and oxygen metabolism in Streptococcus faecalis and comparisons with other organisms.

Authors:  L Britton; D P Malinowski; I Fridovich
Journal:  J Bacteriol       Date:  1978-04       Impact factor: 3.490

2.  Preparation and assay of superoxide dismutases.

Authors:  J D Crapo; J M McCord; I Fridovich
Journal:  Methods Enzymol       Date:  1978       Impact factor: 1.600

3.  Superoxide dismutases in polymorphonuclear leukocytes.

Authors:  M L Salin; J M McCord
Journal:  J Clin Invest       Date:  1974-10       Impact factor: 14.808

4.  Iron containing superoxide dismutases from luminous bacteria.

Authors:  K Puget; A M Michelson
Journal:  Biochimie       Date:  1974       Impact factor: 4.079

5.  Isolation of a new copper-containing superoxide dismutase bacteriocuprein.

Authors:  K Puget; A M Michelson
Journal:  Biochem Biophys Res Commun       Date:  1974-06-04       Impact factor: 3.575

6.  Evidence for a natural gene transfer from the ponyfish to its bioluminescent bacterial symbiont Photobacter leiognathi. The close relationship between bacteriocuprein and the copper-zinc superoxide dismutase of teleost fishes.

Authors:  J P Martin; I Fridovich
Journal:  J Biol Chem       Date:  1981-06-25       Impact factor: 5.157

7.  Superoxide dismutase: improved assays and an assay applicable to acrylamide gels.

Authors:  C Beauchamp; I Fridovich
Journal:  Anal Biochem       Date:  1971-11       Impact factor: 3.365

8.  Isolation and characterization of a protein with cyanide-sensitive superoxide dismutase activity from the prokaryote, Paracoccus denitrificans.

Authors:  P M Vignais; A Terech; C M Meyer; M F Henry
Journal:  Biochim Biophys Acta       Date:  1982-03-04

9.  Copper-zinc superoxide dismutase from Caulobacter crescentus CB15. A novel bacteriocuprein form of the enzyme.

Authors:  H M Steinman
Journal:  J Biol Chem       Date:  1982-09-10       Impact factor: 5.157

10.  The primary structure of Cu-Zn superoxide dismutase from Photobacterium leiognathi: evidence for a separate evolution of Cu-Zn superoxide dismutase in bacteria.

Authors:  G J Steffens; J V Bannister; W H Bannister; L Flohé; W A Günzler; S M Kim; F Otting
Journal:  Hoppe Seylers Z Physiol Chem       Date:  1983-06
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  7 in total

1.  Copper, Zinc-Superoxide Dismutase from Clinically Isolated Escherichia coli: Cloning, Analysis of sodC and Its Possible Role in Pathogenicity.

Authors:  M K Sanjay; S M Srideshikan; V L Vanishree; M S Usha; A Philip Raj; S M Gaddad; C T Shivannavar
Journal:  Indian J Microbiol       Date:  2011-01-26       Impact factor: 2.461

2.  Periplasmic superoxide dismutases in Aquaspirillum magnetotacticum.

Authors:  K A Short; R P Blakemore
Journal:  Arch Microbiol       Date:  1989       Impact factor: 2.552

3.  Superoxide Dismutase Activity in Needles of Norwegian Spruce Trees (Picea abies L.).

Authors:  A Polle; B Krings; H Rennenberg
Journal:  Plant Physiol       Date:  1989-08       Impact factor: 8.340

4.  Periplasmic superoxide dismutase in meningococcal pathogenicity.

Authors:  K E Wilks; K L Dunn; J L Farrant; K M Reddin; A R Gorringe; P R Langford; J S Kroll
Journal:  Infect Immun       Date:  1998-01       Impact factor: 3.441

5.  Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae.

Authors:  J S Kroll; P R Langford; B M Loynds
Journal:  J Bacteriol       Date:  1991-12       Impact factor: 3.490

6.  Evolution of a tRNA operon in gamma purple bacteria.

Authors:  S Giroux; R Cedergren
Journal:  J Bacteriol       Date:  1989-12       Impact factor: 3.490

7.  Iron is a signal for Stenotrophomonas maltophilia biofilm formation, oxidative stress response, OMPs expression, and virulence.

Authors:  Carlos A García; Eliana S Alcaraz; Mirta A Franco; Beatriz N Passerini de Rossi
Journal:  Front Microbiol       Date:  2015-09-04       Impact factor: 5.640

  7 in total

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