Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Alan M. Nigen"'
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
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
Publikováno v:
Journal of Biological Chemistry. 247:4100-4102
Cyanoferrimyoglobins of sperm whale and harbor seal, and bovine pancreatic ribonuclease A have been carboxymethylated with enriched [2-13C]bromoacetate. In each case the contribution of the enriched adduct was clearly discernible by 13C nuclear magne
Studies on the effect of chloride on the oxygen equilibrium of a hemoglobin derivative specifically carbamylated at Val-1 (β) have indicated that this residue is not a major, oxygen-linked binding site for this anion. The postulate that Lys-82 (β)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::24b14493476f34135c515f92f6cd73a4
https://doi.org/10.1016/b978-0-12-164350-8.50055-8
https://doi.org/10.1016/b978-0-12-164350-8.50055-8
Autor:
James M. Manning, Alan M. Nigen
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 74(1)
Concentrations of DL-glyceraldehyde between 5 and 20 mM reduce the sickling of S/S erythrocytes even in the complete absence of oxygen; at 10 mM glyceraldehyde the increase in the number of normal cells ranges from 20 to 40%. The inhibition of sickli