Zobrazeno 1 - 10
of 180
pro vyhledávání: '"F, Taketa"'
Publikováno v:
Hemoglobin. 2:371-381
The two major hemoglobins found in domestic cat blood occur within the same erythrocyte. A putative asymmetrical hybrid, alpha2betaAbetaB, is shown to be present in the cell by isoelectric focusing.
Publikováno v:
Journal of Inorganic Biochemistry. 25:95-108
The location of the various copper binding sites for horse and human hemoglobin was probed using spin labels attached to the β-93 cysteine residue. Dipole-dipole interactions between the spin label and bound copper produce a decrease in the amplitud
Publikováno v:
Comparative Biochemistry and Physiology Part A: Physiology. 56:499-502
1. 1. Whole blood pH was monitored continuously during the generation of oxyhemoglobin dissociation curves with pH electrodes attached to a dissociation curve analyzer. 2. 2. Samples of whole blood drawn from non-smoking human adults showed a non-lin
Publikováno v:
Archives of Biochemistry and Biophysics. 203:466-472
Binding of triethyltin to the cat hemoglobins (HbA and HbB) results in the “masking” of two of the freely reactive sulfhydryl groups (SH) within the hemoglobin tetramer. That the “masked” SH groups occur in position 13α of each α-subu
Publikováno v:
Biochemical and Biophysical Research Communications. 75:389-393
Inositol hexaphosphate (IHP) 1 increases the rate of the NADH-methemoglobin reductase reaction at neutral pH. This effect is apparently associated with the change in conformation of methemoglobin induced by its interaction with IHP. It is consistent
Autor:
F Taketa, K R Siebenlist
Publikováno v:
Journal of Biological Chemistry. 258:11384-11390
Triethyltin bromide activates the cyclic AMP-dependent protein kinases of human red cell membranes and of bovine brain. Additions of 25-500 microM triethyltin to red cell ghosts resulted in enhanced phosphorylation of ghost proteins. When added to pa
Autor:
K.R. Siebenlist, F. Taketa
Publikováno v:
Toxicology and Applied Pharmacology. 58:67-75
Triethyltin bromide interacts with the cat hemoglobin and increases its oxygen affinity. The bound complex was visualized by isoelectric focusing on acrylamide gels. Human and trout hemoglobins showed no evidence of interaction with the reagent when
Autor:
F. Taketa, Jane Kasten-Jolly
Publikováno v:
Archives of Biochemistry and Biophysics. 214:829-839
Acetylation of the amino-terminal serine of the β chains of cat hemoglobin B (HbB) occurs during synthesis of hemoglobin in a mRNA-dependent protein synthesizing system from rabbit reticulocyte lysate in the presence of acetyl-CoA and cat reticulocy
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 400:348-353
The characterization of hemoglobin Wood (beta97(FG4) His replaced by Leu), a high oxygen affinity hemoglobin with reduced Hill constant is described. The amino acid substitution occurs at the alpha1beta2 interface, in the same position as in hemoglob
Autor:
Jane Kasten-Jolly, F. Taketa
Publikováno v:
Biochemical Genetics. 22:901-911
The molecular basis for the genetic control of variable proportions of the two hemoglobins in domestic cat blood was investigated. Both major hemoglobins of cat blood, HbA (α2β 2 A ) and HbB (α2β 2 B ), were synthesized in an mRNA-dependent rabbi