ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

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
Filter
  • nitrotyrosine  (2)
  • 2-phenylglycerol  (1)
  • 1
    Electronic Resource
    Electronic Resource
    2-Phenylglycerol: crystal structure and conformational considerations pertaining to formation of its related oxetane (2000)
    Springer
    Journal of chemical crystallography 30 (2000), S. 83-90 
    Details
    ISSN: 1572-8854
    Keywords: 2-phenylglycerol ; x-ray structure ; computational studies ; conformations
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract 2-Phenylglycerol has been crystallized, structurally characterized, and its related conformations considered by ab initio calculations at the HF/6-31G* level. C9H12O3. $$ \frac{1}{2} $$ H2O, P21,a = 5.8786(1), b = 28.6605(7), c = 10.5553(3) Å, β = 90.187 (1)° at 100(1) K, Z = 8, R = 0.0424 for 5913 unique observed reflections. The asymmetric unit contains four molecules of the title compound and two molecules of water. The structures are characterized by extensive intermolecular hydrogen bonds. The packing is dominated by a hydrophilic hydrogen bonded layer with the hydrophobic phenyl rings forming a herringbone packed intermediate layer. Computational studies suggest that an increase in energy of about 13 kcal/mol can provide for significant conformational flexibility, including the traversal of an orientation that is appropriately aligned with the reaction trajectory needed for closure to the oxetane. Progression along this reaction coordinate, however, will probably require at least another 15 kcal/mol in the gas phase in order to bring the two SN2 species into a proximity which approaches that of the oxetane's C-O bond distance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009558410259
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Denitration of peroxynitrite-treated proteins by ‘protein nitratases’ from rat brain and heart (1999)
    Springer
    Molecular and cellular biochemistry 201 (1999), S. 11-16 
    Details
    ISSN: 1573-4919
    Keywords: peroxynitrite ; nitrotyrosine ; denitration-enzyme/nitratase ; glutathione S-transferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Putative ‘protein nitratases’, which catalyze denitration of peroxynitrite (PN)-treated proteins, were detected in the homogenate/crude extract of rat brains and hearts. Nitratase activity was monitored by the decreased intensity of nitrotyrosine immunoreactive-bands in Western blot and increased nitrate level in dialysate of incubation mixture, which contained homogenate/crude extract, protease inhibitors and a PN-treated substrate, such as treated histone (III-S), BSA or invertase. Enhanced activity of nitratases was noted by preincubating crude extract with Ca2+. In addition, at least two types of nitratases may occur: type I, reductant-dependent, and type II, reductant- independent. Furthermore, upon denitration, the activity of PN-treated invertase increased to the same activity level of the untreated invertase. The overall reaction catalyzed by nitratases for denitration of nitrotyrosine residues in protein could be as follows: Protein-Tyr-NO_2 + H2O → Protein-Tyr-H + H+ + NO3 −. The nitration/denitration of protein-tyrosine may be crucial in regulating signal transduction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007024126947
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Protein nitration (2000)
    Springer
    Molecular and cellular biochemistry 214 (2000), S. 121-129 
    Details
    ISSN: 1573-4919
    Keywords: peroxynitrite ; nitrotyrosine ; nitric oxide ; protein nitration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Various proteins/enzymes obtained commercially were tested for the presence of endogenously nitrated tyrosine by Western blot analysis omitting reducing agent in the step of SDS-PAGE. Histones II-S and VIII-S, IgG, cAMP-dependent protein kinase (PKA), phosphorylase b, and phosphorylase kinase exhibited strong immunoreactive bands. Histone VI-S, glycogen synthase, lactate dehydrogenase, actin, thyroglobulin, and macroglobulin exhibited moderate immunoreactivity. Histone III-S, casein, acetyl cholinesterase, DNase I, and lipase had only traceable immunoreactivity. Whereas histone VII-S, pyruvate kinase, trypsin, pepsin, chymotrypsin, protease IV, and protease XIII, and glutathione S-transferase lacked immunoreactivity. A variation of immunoreactivity between hypertensive and normaltensive rat hearts was found in the histone-agarose fractions of crude extracts. Additionally, nitrotyrosine immunoreactivity was observed in non-mammalian organisms including Eschericia coli, Saccharomyces cerevisiae and Triticum vulgaris. Upon the treatment of 15 μM peroxynitrite (PN), strong oxidant derived from nitric oxide (NO), the apparent Km of PKA for cAMP increased from approximately 10-8 to 10-6 M. The results imply that the varied nitration of tyrosine residues in proteins/enzymes may occur as a post-translational modification in vivo, and such discriminative nitration may be vital in PN/NO-regulated signal transduction cascade.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007118300731
    Location Call Number Expected 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...