Zobrazeno 1 - 10
of 27
pro vyhledávání: '"A M, Nigen"'
Autor:
null B. Agyemang, null J. Grabulos, null O. Hubert, null C. Bourlieu, null M. Nigen, null M. Lebrun, null F. Coffigniez, null V. Guillard, null P. Brat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5bcf5339cb856234dd76816f4427f00c
https://doi.org/10.1111/ijfs.15865/v3/response1
https://doi.org/10.1111/ijfs.15865/v3/response1
Autor:
Thierry Doco, D. Renard, M. Nigen, Chloé Amine, Christian Sanchez, Pascale Williams, V. Mejia Tamayo
Publikováno v:
Food Hydrocolloids
Food Hydrocolloids, Elsevier, 2018, 78, pp.140-160. ⟨10.1016/j.foodhyd.2017.04.008⟩
Food Hydrocolloids (78), 140-160. (2018)
Food Hydrocolloids, Elsevier, 2018, 78, pp.140-160. ⟨10.1016/j.foodhyd.2017.04.008⟩
Food Hydrocolloids (78), 140-160. (2018)
On behalf of the 90th birthday of Professor Glyn O. Phillips, it is a great honor for authors of this publication to make a review on Acacia gum, one of the favorite polysaccharides extensively studied by Glyn and his collaborators all around the wor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8c887fe258dc09b1cf1518e2303f152
https://hal.archives-ouvertes.fr/hal-01602791/file/Sanchez-FH-2017-manuscript-IATE-SPO_1.pdf
https://hal.archives-ouvertes.fr/hal-01602791/file/Sanchez-FH-2017-manuscript-IATE-SPO_1.pdf
Publikováno v:
Journal of Biological Chemistry. 249:6611-6616
Tetramers of hemoglobin S carbamylated on the NH2-terminal residues of the α chains (α2cβ2), the β chains (α2β2c), or both chains (α2cβ2c) have been prepared. For this purpose carbamylation was carried out with deoxyhemoglobin to yield a prod
Publikováno v:
Journal of Biological Chemistry. 249:4149-4156
Pentapeptides containing either l-methionine, l-proline, l-arginine, or l-lysine as central residue in the pattern glycylglycyl-X-glycylglycine have been studied at natural abundance by proton-decoupled 13C nuclear magnetic resonance spectroscopy. Re
Publikováno v:
Journal of Biological Chemistry. 255:5525-5529
A hemoglobin hybrid (alpha 2c beta 2 Prov) in which the alpha chains have NH2-terminal residues that have been blocked specifically by carbamylation and beta chains that have been derived from hemoglobin Providence I (beta 82 Lys leads to Asn) was pr
Publikováno v:
Journal of Biological Chemistry. 251:7638-7643
The 3-fold increase in the carbamylation rate of Val-1 (alpha) of hemoglobin upon deoxygenation described earlier is now shown to be a sensitive probe of conformational change. Thus, whereas this residue in methemoglobin A is carbamylated at the same
Autor:
Frank R. N. Gurd, Alan M. Nigen
Publikováno v:
Journal of Biological Chemistry. 248:3708-3715
Harbor seal (Phoca vitulina) and sperm whale (Physeter catodon) myoglobins were carboxymethylated in 0.2 m bromoacetate at pH 6.8. The modification of histidine residues leveled off after approximately 6 and 8 days, respectively, of reaction at 25°
Autor:
Jon S. Morrow, Robert C. Marshall, Robert A. Vigna, Philip Keim, Alan M. Nigen, Frank R. N. Gurd
Publikováno v:
Journal of Biological Chemistry. 248:3724-3732
Cyanoferrimyoglobins of harbor seal and sperm whale were carboxymethylated with enriched [2-13C] bromoacetate. The enriched adducts were readily observed by 13C nuclear magnetic resonance. Resonances were identified by comparison with enriched adduct
Autor:
Frank R. N. Gurd, Peter J. Lawson, Alan M. Nigen, Philip Keim, Victor Glushko, Robert C. Marshall
Publikováno v:
Journal of Biological Chemistry. 248:3716-3723
Proton-decoupled Fourier transform nuclear magnetic resonance of natural abundance 13C was used to obtain spectra of cyanoferrimyoglobins of harbor seal (Phoca vitulina) and sperm whale (Physeter catodon). These spectra were compared with those of he
Autor:
James M. Manning, Peter N. Gillette, Njifutei Njikam, Wanda M. Jones, Alan M. Nigen, Robley C. Williams
Publikováno v:
Journal of Biological Chemistry. 248:8052-8056
Carbamylation of the NH2-terminal valine residues of hemoglobin by cyanate in vitro is about 2½ times as extensive in partially deoxygenated whole blood (40 to 50% oxygen saturation) as in fully oxygenated whole blood. When the carbamylated α and