Zobrazeno 1 - 10
of 10
pro vyhledávání: '"L B, Poole"'
Publikováno v:
European journal of biochemistry. 267(20)
A group of bacterial flavoproteins related to thioredoxin reductase contain an additional approximately 200-amino-acid domain including a redox-active disulfide center at their N-termini. These flavoproteins, designated NADH:peroxiredoxin oxidoreduct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1305603c7b7819d4ff8c4b770b890078
https://pubmed.ncbi.nlm.nih.gov/11012664
https://pubmed.ncbi.nlm.nih.gov/11012664
Publikováno v:
Free radical biologymedicine. 23(6)
The 29 kDa surface protein of Entamoeba histolytica is an abundant antigenic protein expressed by pathogenic strains of this organism. The protein is a member of a widely-dispersed group of homologues which includes at least two cysteinyl peroxidases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::010b11a79799e157238dff3874f2ca97
https://pubmed.ncbi.nlm.nih.gov/9378375
https://pubmed.ncbi.nlm.nih.gov/9378375
Publikováno v:
Biochemistry. 30(15)
It has been shown (Poole et al., 1991) that deletion of residues 44-49 from the sequence of staphylococcal nuclease (E43 SNase) results in an enzyme (E43 delta SNase) that is significantly more active than D43 SNase, an enzyme that differs from the w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c501c6efa08a982ff06f107c37e09248
https://pubmed.ncbi.nlm.nih.gov/2015220
https://pubmed.ncbi.nlm.nih.gov/2015220
Publikováno v:
Biochemistry. 30(15)
The high-resolution X-ray structure of wild-type staphylococcal nuclease (E43 SNase) suggests that Glu 43 acts a general basic catalyst to assist the attack of water on a phosphodiester substrate [Loll, P.,Lattman, E. E. (1989) Proteins: Struct., Fun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bf7438fdfeadabaff04bad99424bc4a1
https://pubmed.ncbi.nlm.nih.gov/2015219
https://pubmed.ncbi.nlm.nih.gov/2015219
Autor:
A Claiborne, L B Poole
Publikováno v:
Journal of Biological Chemistry. 261:14525-14533
The flavin-containing NADH peroxidase of Streptococcus faecalis 10C1, which catalyzes the reaction: NADH + H+ + H2O2----NAD+ + 2H2O, has been purified to homogeneity in our laboratory for analyses of both its structure and redox behavior. Our finding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::05b344a7221440268f3bb9693d7b288a
https://doi.org/10.1016/s0021-9258(18)66901-7
https://doi.org/10.1016/s0021-9258(18)66901-7
Autor:
L B, Poole, A, Claiborne
Publikováno v:
Biochemical and biophysical research communications. 153(1)
Substrate reduction of the streptococcal flavoprotein NADH peroxidase, followed by anaerobic denaturation and titration with 5,5'-dithiobis(2-nitrobenzoate), yields a stoichiometry of one protein thiol per mole of FAD. Analysis of the NADH peroxidase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5300bb2cc9d4f3bddca167c2b0f45caf
https://pubmed.ncbi.nlm.nih.gov/3132163
https://pubmed.ncbi.nlm.nih.gov/3132163
Autor:
L B, Poole, A, Claiborne
Publikováno v:
The Journal of biological chemistry. 264(21)
Unlike the 2-electron-reduced (EH2) forms of the flavoprotein disulfide reductases and mercuric reductase, the native EH2 form of the streptococcal NADH peroxidase is quite refractile toward chemical modification with thiol-specific reagents. In the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::273f0dcde1e26711c92fbbf480c8c56c
https://pubmed.ncbi.nlm.nih.gov/2501302
https://pubmed.ncbi.nlm.nih.gov/2501302
Autor:
L B, Poole, A, Claiborne
Publikováno v:
The Journal of biological chemistry. 264(21)
Incubation of the streptococcal NADH peroxidase with 5-thio-2-nitrobenzoate under anaerobic denaturing conditions leads to the rapid incorporation of 1 eq/FAD of the aromatic thiol. Addition of dithiothreitol to the resulting conjugate, following ult
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ce2b3a16c92ea9d95c7b3c41573404d8
https://pubmed.ncbi.nlm.nih.gov/2501303
https://pubmed.ncbi.nlm.nih.gov/2501303
Autor:
L B, Poole, A, Claiborne
Publikováno v:
The Journal of biological chemistry. 261(31)
The flavin-containing NADH peroxidase of Streptococcus faecalis 10C1, which catalyzes the reaction: NADH + H+ + H2O2----NAD+ + 2H2O, has been purified to homogeneity in our laboratory for analyses of both its structure and redox behavior. Our finding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ebb90a14e35ddee09af0c4ec848aab63
https://pubmed.ncbi.nlm.nih.gov/3095321
https://pubmed.ncbi.nlm.nih.gov/3095321
Publikováno v:
The American journal of physiology. 247(5 Pt 2)
Kinetic analyses of the Na+-K+-adenosine triphosphatase (ATPase) system were performed in brain and heart preparations from young mature (4 mo old) and healthy aged (25 mo old) rats. The K+-activated p-nitrophenylphosphatase (K+-pNPPase) method was u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb7cee0b1cedb37f73ee2f1bc6030f22
https://pubmed.ncbi.nlm.nih.gov/6093604
https://pubmed.ncbi.nlm.nih.gov/6093604