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At least 73 records · Page 4Linked to original sources
PubMed1975

Use of leuco-dyes in the quantitative colorimetric microdetermination of hemoglobin and other heme compounds.

Sensitivity, stability, and specificity of the color-producing reaction of hydrogen peroxide with bezidine, leuco-malachite green, or o-dianisidine were tested in numerous systems containing hemoglobin and other hemoproteins. Use of urea or low temperature (to minus 12 degrees C), or both, was highly beneficial, especially with leuco-malachite green, for which the color reaction was stable, after about 15 min, for longer than 24 h, with a colorless bank. Absorbance was 0.3 at a final hemoglobin concentration of 0.27 mg/liter. Nonspecific color produced by substances such as FeCl-3 and ascorbic acid was completely eliminated. Of the three leuco-dyes studied, only benzidine yielded a completely linear calibration curve, but its relative instability and reported carcinogenicity are serious disadvantages. No system tested eliminated completely the known inhibition by plasma of the peroxidase activity of these leuco dyes.

Colorimetry↗
PubMed1988

Bonding of nitrosobenzene and phenyl isocyanide to chelated mesoheme, hemoglobin and ferrous phthalocyanine.

Reactions of nitrosobenzene, phenyl isocyanide and their ring-substituted analogues with hemoglobin, ferrous phthalocyanine and a synthetic model compound of hemoglobin were investigated by optical, 1H-NMR and infrared spectroscopy. Complexes of chelated ferromesoheme, the model compound, with 2-methyl-, 2-ethyl, 2-isopropyl- or 2,6-disubstituted nitrosobenzene were less stable than its complex with nitrosobenzene. Formation of a complex of the model compound with 2-tert-butylnitrosobenzene was incomplete. Previous studies showed that 2,6-disubstituted nitrosobenzenes are not ligands of ferrohemoglobin. In the present work 2,6-dimethylphenyl isocyanide was found to be a ligand of ferrohemoglobin. These results are consistent with binding of the nitrogen of the nitroso group of nitrosobenzene and of the carbon of the isocyanide group of phenyl isocyanide to ferroheme. The same bonding modes of these ligands to ferrous phthalocyanine were inferred from ring-current-induced shifts in the 1H-NMR spectra of the respective complexes.

Chlorides↗
PubMed2000

Fetal hemoglobin expression in the compound heterozygous state for -117 (G-->A) Agamma HPFH and IVS-1 nt 110 (G-->A) beta+ thalassemia: a case study.

The splicing defect at IVS-I-110 is by far (43.15%) the most common beta-thalassaemia mutation in Greece. The - 117 (G-->A) Agamma hereditary persistence of fetal hemoglobin (Greek HPFH) is also the most frequent nondeletional HPFH in Greece. We report a case in which these two defects co-segregates. She is a healthy female where the total Hb is 12.3 g/dl with 51% HbF and normal HbA2. Her Ggamma/Agamma ratio is 35:65 differing from that of 10 simple heterozygotes for the Greek HPFH who have ratio of 8:92. Molecular analysis of the beta-globin genotype revealed the presence of the IVS-I-110 beta+ mutation in trans to the -117 G-->A Greek HPFH. Both mutations are linked to Ia. Her father has Greek HPFH in trans to the -158 C-->T on the Ggamma promoter, which is linked with haplotype IIIalpha. He has 13% HbF with a Ggamma/Agamma ratio 32:68. Her sister is a compound heterozygote for the IVS-I-110 mutation in trans to the - 158 C-->T, with HbF levels of 3% and a Ggamma/Agamma ratio 72:28.

Adult↗
PubMed1952

Sulfhydryl groups and the interaction between the hemes in hemoglobin.

1. Dialysis of a hemoglobin solution against slightly alkaline buffer (pH 8.68) causes a decrease in heme-heme interaction. The value of n in Hill's equation drops from 2.9 to 2.0, while the oxygen affinity increases slightly. Addition of glutathione largely reverses the effects of dialysis (n rises from 2.0 to 2.5 to 2.6). 2. Addition of the sulfhydryl reagent, p-chloromercuribenzoate (1.8 x 10(-3)M), results in a large though not complete blocking of heme-heme interaction. The value of n drops from 2.9 to 1.4. This effect is largely reversed with glutathione (n rises to 2.6).

Glutathione↗
PubMed1956

Sulfhydryl groups and the structure of hemoglobin.

1. Addition of 2 moles of mersalyl, mercuric chloride, p-chloromercuribenzoate (PCMB), or methyl mercury hydroxide per mole of hemoglobin greatly reduces heme-heme interactions (n), yet these substances have quite different effects on the oxygen affinity (-log p(50)). Mersalyl and mercuric chloride at this concentration each increase the oxygen affinity, while PCMB and methyl mercury have little or no effect on the oxygen affinity. These effects are primarily associated with the binding of -SH groups, and are largely reversed on the addition of glutathione. -SH groups do not appear to be responsible for the Bohr effect. 2. Evidence is presented for the belief that the two hemes of each half-molecule of horse hemoglobin are situated on either side of a cluster of-SH groups. 3. The mechanism of interaction between the hemes is discussed. It is concluded that the reorganization of the protein architecture which accompanies oxygenation plays a central role in this interaction, in agreement with the views of Pauling and Wyman.

Animals↗
PubMed2001

A comparative study of Greek nondeletional hereditary persistence of fetal hemoglobin and beta-thalassemia compound heterozygotes.

The coexistence of beta- and gamma-globin gene mutations in the compound heterozygous state presents a rare in vivo model that provides important data on gene regulation of clinical interest. In this unique comparative study we present the hematological, biosynthetic, and molecular data from six adult compound heterozygotes for the Greek nondeletional hereditary persistence of fetal hemoglobin (nd-HPFH, Agamma-117 G-->A) and four frequent beta-thalassemia mutations (IVS I-110 G-->A, Cd 39 C-->T, IVS I-1 G-->A, and IVS I-6 T-->C) found in the Hellenic population. Fetal hemoglobin (HbF) levels were found to be considerably higher (25-50%) than in 19 Greek nd-HPFH heterozygotes (HbF=9.7+/-1.7%) and, interestingly, to depend on the type of the respective beta-thalassemia mutation, in trans to the nd-HPFH allele. All cases presented a typical beta-thalassemia heterozygote's phenotype despite the increased HbF and the normal HbA2 levels, as indicated by both the hematological indices and the biosynthetic ratios. These data were compared with those from two unique cases of Greek origin: a homozygous case of the Greek nd-HPFH and a compound heterozygote with HbS. Our data suggest that in these compound heterozygous cases the beta-thalassemic chromosome indirectly determines the final outcome of the gamma- and of the in cis beta-globin gene expression, most likely at the post-transcriptional level.

Adult↗