Zobrazeno 1 - 10
of 37
pro vyhledávání: '"R. Cashon"'
Autor:
J. B. Paine, N. Hill, R. Cashon, J. A. Fournier, Douglas M. Ruthven, D. Cassidy, William J. DeSisto
Publikováno v:
Industrial & Engineering Chemistry Research. 47:7857-7861
We report the synthesis and characterization of a selective nitric oxide (NO) adsorbent based on the covalent binding of cobalt(II) phthalocyanine tetrasulfonic acid (CoPcS) onto imidazole-function...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c325658dd0e4c884555048d1f83685f
https://doi.org/10.1021/ie8000293
https://doi.org/10.1021/ie8000293
Publikováno v:
Journal of Non-Crystalline Solids. 333:143-149
Hemoglobin and myoglobin were encapsulated in silica gels and powders. Protein encapsulated powders were fabricated via the condensation of silicic acid around the protein, followed by a fast freezing with liquid nitrogen, and subsequent thawing. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e58e4426e99db1006744b20646079c3
https://doi.org/10.1016/j.jnoncrysol.2003.09.061
https://doi.org/10.1016/j.jnoncrysol.2003.09.061
Publikováno v:
Journal of Biological Chemistry. 266:17898-17903
The dimeric hemoglobin isolated from Scapharca inaequivalvis, HbI, is notable for its highly cooperative oxygen binding and for the unusual proximity of its heme groups. We now report that the oxidized protein, an equilibrium mixture of a dimeric hig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab883151c22e4c0d1bd09f2db3148764
https://doi.org/10.1016/s0021-9258(18)55212-1
https://doi.org/10.1016/s0021-9258(18)55212-1
Publikováno v:
The Journal of biological chemistry. 267(7)
Heat-shocked organisms are known to produce not only "heat shock proteins" but also diadenosine tetraphosphate (Ap4A) and related compounds that may act as "alarmones" that alert the cell to the onset of metabolic stress. We found that Ap4A is synthe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9e452c4a33b98140a9e3a7eb793dadbe
https://pubmed.ncbi.nlm.nih.gov/1537848
https://pubmed.ncbi.nlm.nih.gov/1537848
Publikováno v:
The Journal of biological chemistry. 266(34)
Hemoglobin (Hb) Chico (Lys beta 66----Thr at E10) has a diminished oxygen affinity (Shih, D. T.-b., Jones, R. T., Shih, M. F.-C., Jones, M. B., Koler, R. D., and Howard, J. (1987) Hemoglobin 11, 453-464). Our studies show that its P50 is about twice
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2db643acf2448c9562ea2c2535f748de
https://pubmed.ncbi.nlm.nih.gov/1744099
https://pubmed.ncbi.nlm.nih.gov/1744099
Autor:
W. J. DeSisto, R. Cashon, D. Cassidy, N. Hill, D. M. Ruthven, J. B. Paine III, J. A. Fournier
Publikováno v:
Industrial & Engineering Chemistry Research; Sep2008, Vol. 47 Issue 20, p7857-7861, 5p
Publikováno v:
Journal of Biological Chemistry. 264:11302-11306
Spectrofluorometric techniques were used to quantify NADPH-hemoglobin interactions based on the quenching of NADPH fluorescence upon binding to hemoglobin. Fluorometric titrations were carried out with hemoglobin in varied states and with hemoglobins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18fb38963e49ef394b07481a0fffc4cc
https://doi.org/10.1016/s0021-9258(18)60464-8
https://doi.org/10.1016/s0021-9258(18)60464-8
Publikováno v:
Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas. 20(6)
The affinity constants for the binding of NADPH to human hemoglobin A were directly determined by fluorescence analysis since nucleotide fluorescence is quenched on binding to the protein. The binding constants 6.1 x 10(5), 5.02 x 10(5) and 1.2 x 10(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::203faf8e9d62c0ae56f4a8cf09ac5b87
https://pubmed.ncbi.nlm.nih.gov/3455253
https://pubmed.ncbi.nlm.nih.gov/3455253
Publikováno v:
The Journal of biological chemistry. 264(19)
Spectrofluorometric techniques were used to quantify NADPH-hemoglobin interactions based on the quenching of NADPH fluorescence upon binding to hemoglobin. Fluorometric titrations were carried out with hemoglobin in varied states and with hemoglobins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c385d201d2ab724d57705aca37f73fdd
https://pubmed.ncbi.nlm.nih.gov/2738066
https://pubmed.ncbi.nlm.nih.gov/2738066
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