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PubMed1980

Immunochemical properties of abnormal hemoglobins C-Harlem (beta 6 Glu replaced by Val, beta 73 Asp replaced by Asn), S (beta 6 Glu replaced by Val), Korle Bu (beta 73 Asp replaced by Asn), Vancouver (beta 73 Asp replaced by Tyr), and Mobile (beta 73 Asp replaced by Val).

Antibodies were made to three mutant hemoglobins, each containing different single amino acid substitutions at beta 73:Hb Korle Bu (Asp replaced by Asn), Hb Mobile (Asp leads to Val), Hb Vancouver (Asp replaced by Tyr); and to one mutant hemoglobin, Hb C-Harlem, containing two substitutions in the beta chain (beta 6 Glu replaced by Val, as in Hb S, and beta 73 Asp replaced by Asn, as in Hb Korle Bu). The antiserum to Hb C-Harlem contained two antibody populations, each specific for one mutant amino acid residue. The antiserum to Hb Vancouver was completely specific for this mutant and did not cross-react with Hb Mobile and Hb Korle Bu; however, antiserum to Hb Korle Bu partially cross-reacted with Hb Mobile and to a smaller degree with Hb Vancouver. Antiserum to Hb Mobile exhibited even less cross-reactivity with Hb Korle Bu and C-Harlem and none with Hb Vancouver. These and previous studies indicate the involvement of at least three independent areas in the beta chain as antigenic determinant sites. It appears that the three mutants at beta 73 elicit the formation of antibodies which have a gradation in their specificity due to the nature of the amino acid sidechain.

Amino Acids↗
PubMed1993

Capillary electrophoresis of abnormal hemoglobins associated with alpha-thalassemias.

Capillary electrophoresis was evaluated for separation of hemoglobin species associated with alpha-thalassemias, and for identification of hemoglobin variants commonly found in the same human populations. Separation of hemoglobins was achieved using capillary isoelectric focusing with chemical mobilization; visible-wavelength absorbance detection was used to identify hemoglobins against a background of nonheme-containing proteins. This technique could easily differentiate hemoglobins Bart's and H (associated with alpha-thalassemias) from hemoglobin variants. Analysis of globin chains derived from intact hemoglobins was performed by free zone capillary electrophoresis under denaturing conditions. This technique was useful for distinguishing Hb Bart's and Hb H, and for confirming the identity of hemoglobin variants.

Electrophoresis↗
PubMed1985

Hb Doha or alpha 2 beta 2[X-N-Met-1(NA1)Val----Glu]; a new beta-chain abnormal hemoglobin observed in a Qatari female.

Structural analysis of a fast-moving hemoglobin variant, present in three members of a Qatari family, identified a Val----Glu substitution at position 1 (NA1) of the beta-chain. The introduction of this glutamic acid residue prevents the removal of the initiator methionine, thus extending the N-terminus by one residue to Met-Glu-His-Leu-Thr-. The methionine residue is blocked by an as yet not completely identified molecule. The presence of the variant in a heterozygote does not have clinical consequences.

Adult↗
PubMed1982

A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket.

Proton nuclear magnetic resonance spectroscopy at 250 MHz has been used to investigate the conformations of proximal histidyl residues of human normal adult hemoglobin, hemoglobin Kempsey [beta 99(G1) Asp leads to Asn], hemoglobin Osler [beta 145(HC2) Tyr leads to Asp], and hemoglobin McKees Rocks [beta 145(HC2) Tyr leads to Term] around neutral pH in H2O at 27 degrees C, all in the deoxy form. Two resonances that occur between 58 and 76 ppm downfield from the water proton signal have been assigned to the hyperfine shifted proximal histidyl NH-exchangeable protons of the alpha- and beta-chains of deoxyhemoglobin. These two resonances are sensitive to the quaternary state of hemoglobin, amino acid substitutions in the alpha 1 beta 2-subunit interface and in the carboxy-terminal region of the beta-chain, and the addition of organic phosphates. The experimental results show that there are differences in the heme pockets among these four hemoglobins studied. The structural and dynamic information derived from the hyperfine shifted proximal histidyl NH-exchangeable proton resonances complement that obtained from the ferrous hyperfine shifted and exchangeable proton resonances of deoxyhemoglobin over the spectral region from 5 to 20 ppm downfield from H2O. The relationship between these findings and Perutz's stereochemical mechanism for the cooperative oxygenation of hemoglobin is discussed.

2,3-Diphosphoglycerate↗
PubMed2003

First case of a single heterozygote of an abnormal hemoglobin, Hb Stanmore, [beta111(G13)Val-->Ala].

We describe a hemoglobin beta-chain mutant detected incidentally in an unusual profile of glycated hemoglobin (HbA1c) measured by ion-exchange HPLC. Analysis of intact globin by electrospray ionization mass spectrometry (ESI-MS) and peptide analysis by on-line HPLC-ESI-MS-MS revealed the substitution, [beta111(G13)Val-->Ala], which was confirmed by DNA analysis. This was the second case of Hb Stanmore. As the first case combined beta(0)-thalassemia, and the family study in that case showed no case of Hb Stanmore without combined thalassemia, the case presented here is the first case of single heterozygote, and the first Japanese case. Hb Stanmore is isoelectrophoretically silent with only mild clinical symptoms, although stability by isopropanol test was positive.

Adult↗