Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd1) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans (1996)
    Springer
    Archives of microbiology 165 (1996), S. 55-61 
    Details
    ISSN: 1432-072X
    Keywords: Key words Cytochrome cd1 ; Nitrite reductase ; Nitrous ; oxide reductase ; Denitrification ; Thiobacillus ; denitrificans ; Pseudomonas stutzeri ; DNA hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cytochrome cd 1-nitrite reductase and nitrous oxide reductase of Thiobacillus denitrificans were purified and characterized by biochemical and immunochemical methods. In contrast to the generally soluble nature of the denitrification enzymes, these two enzymes were isolated from the membrane fraction of T. denitrificans and remained active after solubilization with Triton X-100. The properties of the membrane-derived enzymes were similar to those of their soluble counterparts from the same organism. Nitrous oxide reductase activity was inhibited by acetylene. Nitrite reductase and nitrous oxide reductase cross-reacted with antisera raised against the soluble enzymes from Pseudomonas stutzeri. The nirS, norBC, and nosZ genes encoding the cytochrome cd 1-nitrite reductase, nitric oxide reductase, and nitrous oxide reductase, respectively, from P. stutzeri hybridized with genomic DNA from T. denitrificans. Cross-reactivity and similar N-terminal amino acid and gene sequences suggest that the primary structures of the Thiobacillus enzymes are homologous to the soluble proteins from P. stutzeri.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050296
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Identification of a copper protein as part of the nitrous oxide-reducing system in nitrite-respiring (denitrifying) pseudomonads (1982)
    Springer
    Archives of microbiology 132 (1982), S. 322-328 
    Details
    ISSN: 1432-072X
    Keywords: Nitrous oxide reduction ; Copper proteins ; Cytochrome patterns ; Denitrification ; Pseudomonas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Copper is the essential transition element for nitrous oxide respiration in Pseudomonas perfectomarinus. Two novel kinds of copper proteins were detected in this organism. Their distribution was studied under different growth conditions and in other pseudomonads, as well as their association with N2O reduction of intact cells. A low molecular mass copper protein (M r 38,000) with a single absorption band at 340 nm (oxidized form), was found only in P. perfectomarinus and was not required for N2O reduction. N2O respiration was consistently associated with a high molecular mass copper protein (M r 120,000) in P. perfectomarinus, Pseudomonas stutzeri, and in strains of Pseudomonas fluorescens that were capable of this type of respiration. The oxidized protein was violet to pink with absorption bands at 350, 480, 530, 620, and 780 nm. Pseudomonas chlororaphis and Pseudomonas aureofaciens which did not respire with N2O as electron acceptor, did not contain the novel type of copper protein. Cytochrome patterns were compared in these denitrifying pseudomonads to search for the physiological electron carrier to N2O reductase. The content and nature of the soluble c-type cytochromes depended strongly on the species and the particular growth condition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00413383
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Copper-containing nitrite reductase from Pseudomonas aureofaciens is functional in a mutationally cytochrome cd 1-free background (NirS−) of Pseudomonas stutzeri (1993)
    Springer
    Archives of microbiology 160 (1993), S. 18-26 
    Details
    ISSN: 1432-072X
    Keywords: Nucleotide sequence ; Apocytochrome cd 1 ; Heme d 1 incorporation ; Denitrification ; Copper coordination ; Signal peptide ; Escherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The structural gene, nirK, for the respiratory Cu-containing nitrite reductase from denitrifying Pseudomonas aureofaciens was isolated and sequenced. It encodes a polypeptide of 363 amino acids including a signal peptide of 24 amino acids for protein export. The sequence showed 63.8% positional identity with the amino acid sequence of “Achromobacter cycloclastes” nitrite reductase. Ligands for the blue, type I Cu-binding site and for a putative type-II site were identified. The nirK gene was transferred to the mutant MK202 of P. stutzeri which lacks cytochrome cd 1 nitrite reductase due to a transposon Tn5 insertion in its structural gene, nirS. The heterologous enzyme was active in vitro and in vivo in this background and restored the mutationally interrupted denitrification pathway. Transfer of nirK to Escherichia coli resulted in an active nitrite reductase in vitro. Expression of the nirS gene from P. stutzeri in P. aureofaciens and E. coli led to nonfunctional gene products. Nitrite reductase activity of cell extract from either bacterium could be reconstituted by addition of heme d 1, indicating that both heterologous hosts synthesized a cytochrome cd 1 without the d 1-group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00258141
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Enzyme diversity and mosaic gene organization in denitrification (1997)
    Springer
    Antonie van Leeuwenhoek 71 (1997), S. 43-58 
    Details
    ISSN: 1572-9699
    Keywords: Denitrification ; mosaic gene organization ; nitrous oxide reductase ; nitric oxide reductase ; structural models ; cytochrome c oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Denitrification is a main branch of the global nitrogen cycle. In the past ten years unravelling the underlying biochemistry and genetics has proceeded at an increasing pace. Fungal denitrification has become a new field. The biochemical investigation of denitrification has culminated in the description of the crystal structures of the two types of nitrite reductases. The N2O reductase shares with cytochrome c oxidase the CuA center as a structurally novel metal site. The cytochrome b subunit of NO reductase has a striking conservation of heme-binding transmembrane segments versus the subunit I of cytochrome c oxidase. Another putative denitrification gene product shows structural relation to the subunit III of the oxidase. N2O reductase and NO reductase may be ancestors of energy-conserving enzymes of the heme-copper oxidase superfamily. More than 30 genes for denitrification are located in a 〉30-kb cluster in Pseudomonas stutzeri, and comparable gene clusters have been identifi ed in Pseudomonas aeruginosa and Paracoccus denitrificans. Genes necessary for nitrite reduction and NO reduction have a mosaic arrangement with very few conserved locations within these clusters and relative to each other.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1000112008026
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Comparison of two juvenile hormone radioimmunoassays (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 23 (1993), S. 147-152 
    Details
    ISSN: 0739-4462
    Keywords: honey bee ; Apis mellifera ; juvenile hormone ; radioimmunoassay ; hemolymph ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Juvenile hormone from the hemolymph of adult worker honey bees of known age and behavioral status was extracted and analyzed by two different radioimmunoassays in two independent laboratoies. The assays are different in hapten attachment, radiolabeled tracer, and the method by which bound and unbound hormone are separated. Despite these differences in the methods, hormone determinations were in excellent agreement at lower levels (0-50 ng/ml) but diverged as the hormone concentrations increased (〉 50 ng/ml). The relative changes are in good agreement, with a correlation coefficient of 0.97. © 1993 Wiley-Liss, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940230306
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Juvenile hormone regulation of hemolymph juvenile hormone binding protein in the black strain of the tobacco hornworm, Manduca sexta (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 30 (1995), S. 165-176 
    Details
    ISSN: 0739-4462
    Keywords: Lepidoptera ; radioimmunoassay ; enzyme immunoassay ; equilibrium dialysis ; monoclonal antibody ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Numerous studies have demonstrated regulation of specific lepidopteran proteins by pharmacological doses of insect juvenile hormone (JH). In this study, topical application of a 1 pg dose of JH I to fourth stadium larvae of the black (bl) mutant strain of the tobacco hornworm, Manduca sexta, induced a 50% increase in the titer of hemolymph juvenile hormone binding protein (hJHBP). Radioimmunoassay confirmed that JH titers were lower in bl larvae than in wild-type larvae at the time of JH treatment. Enzyme immunoassay analysis of hJHBP titers demonstrated that regulation by JH I was dose-dependent at doses up to 10 pg and that the response was saturated above 100 pg. Western blotting and equilibrium dialysis confirmed these results and demonstrated that hJHBP from bl larvae had the same molecular mass and displayed the same affinity for JH I as hJHBP isolated from wild-type larvae. Time course studies showed that regulation was complex: 1 2 h after JH I treatment, hJHBP titers were twofold lower in treated than in control bl larvae, while 44 h after treatment they were twofold higher. JH I regulation of hJHBP titers in bl larvae was independent of changes in total hemolymph protein. © 1995 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940300207
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Recent advances in radioimmunoassay technology for the juvenile hormones (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 30 (1995), S. 295-306 
    Details
    ISSN: 0739-4462
    Keywords: radioimmunoassay ; JH I ; JH II ; JH III ; hemolymph ; insect hormone ; Manducasexta sexta ; Hyalophora cecropia ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Recent refinements in juvenile hormone radioimmunoassay technology now make this method significantly more sensitive and easier to use. Rabbit poly-clonal antisera against (10R) JH III and racemic JH II have been developed to determine hemolymph hormone titers in the low picogram range. The antisera display minimal cross-reactivity with JH metabolites, JH analogs, and hemolymph lipids. One antiserum recognizes racemic JH I, II, and (10R) III almost equivalently, exhibiting 50% displacement between 100 and 130 pg per tube. Another antiserum is JH II-specific and exhibits 50% displacement at 35 pg per tube. Assay sensitivity has been enhanced by using (10R,11S) [methyl-3H]-JH II of very high specific activity (〉 80 Ci/mmol) generated with Hyalophora cecropia accessory gland S-adenosylmethionine transferase and S-[methyl-3H]-adenosyl-L-methionine. Preparation of biological samples has been simplified with overall recoveries of JH from hemolymph ranging between 60 and 75%. © 1995 Wiley-Liss, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940300215
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...