PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “HEMOGLOBINS, ABNORMAL”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 685 records · Page 38Linked to original sources
PubMed1992

Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant observed in four families from southern Austria.

Two abnormal hemoglobins were accidentally detected by cation exchange high performance liquid chromatography with the Diamat system of Bio-Rad Laboratories; the variants eluted together with the fast-moving Hb A1c. Structural analysis of isolated beta chains and sequence analysis of amplified DNA identified a new variant, i.e. Hb Graz that has a His-->Leu replacement at position 2 of the beta chain, in four healthy, apparently unrelated, adults. The second variant was identical to Hb Sherwood Forest or alpha 2 beta 2(104)(G6)Arg-->Thr; it is believed that this may be the second observation of this abnormal hemoglobin.

Amino Acid Sequence↗
PubMed1996

Poly-N-acetyllactosaminyl saccharide chains of band 3 as determinants for anti-band 3 autoantibody binding to senescent and oxidized erythrocytes.

Natural IgG antibodies to band 3 glycoprotein of erythrocyte membrane (anti-band 3 IgG) are known to bind to senescent erythrocytes, and believed to initiate antibody-dependent phagocytic removal of the senescent cells from blood circulation. Anti-band 3 antibodies also bind to the erythrocytes with hereditary hemoglobin abnormalities such as sickle, beta-thalassemic and hemoglobin Köln erythrocytes. Oxidative stress appears to be responsible for the generation of senescent cell antigen on erythrocytes, to which anti-band 3 antibodies bind, since erythrocytes oxidized in vitro bind anti-band 3 IgG, and various oxidative modifications are observed in senescent erythrocytes as well as the erythrocytes with abnormal hemoglobin. Major antigenic sites of band 3 for anti-band 3 IgG autoantibodies are its sialylated poly-N-acetyllactosaminyl saccharide chains. The poly-N-acetyllactosaminyl saccharide chains on senescent erythrocytes are indeed involved in the antigenic sites on senescent erythrocytes. The finding of the carbohydrate epitopes and possible involvement of oxidative mechanism are compatible with the band 3 clustering hypothesis, in which clustering of band 3 molecules in erythrocyte membrane is supposed to be responsible for effective binding of anti-band 3 IgG to the cell surface, because the carbohydrate epitopes of band 3 can form multivalent epitopes on cell surface when band 3 molecules cluster, and oxidative stress can induce such clusters. Interestingly, poly-N-acetyllactosaminyl chains of band 3 on oxidized erythrocytes are also recognized by macrophages directly. Thus, poly-N-acetyllactosaminyl chains may play dual roles as determinants for recognition by anti-band 3 IgG and by macrophages.

Anion Exchange Protein 1, Erythrocyte↗
PubMed1979

Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2): an unstable variant associated with alpha-thalassemia.

An abnormal hemoglobin variant was detected in a seven-year old Thai girl. The clinical and hematological pictures were indistinguishable from hemoglobin H disease. Upon cellulose acetate electrophoresis at pH 8.5 an abnormal hemoglobin variant was found together with hemoglobins A and H. The variant moved slightly behind HbF and amounted to approximately 9%. Globin chain synthesis studies of peripheral blood reticulocytes incubated with tritiated leucine revealed that the total radioactivity ratio alpha-chain + variant alpha-chain/beta-chain was 0.59, while the ratio variant alpha-chain/beta-chain was 0.12. The variant hemoglobin was somewhat unstable under heat denaturation and in the isopropanol test. Structural studies by component isolation, globin chain separation, peptide mapping and aminoacid analysis of abnormal peptides showed that the leucine residue 109 of the alpha-chain was replaced by arginine. This hemoglobin mutant has not been described before and is named Hemoglobin Suan-Dok.

Adult↗
PubMed1981

[Clinical studies of the erythrocytosis produced by a new hemoglobin with oxygen affinity : Hb Hôtel-Dieu alpha 2A beta 2 Asp replaced by Gly (author's transl)].

A new case of erythrocytosis associated with a high oxygen affinity hemoglobin is reported : the substitution of beta 99 of aspartic acid by glycine, characterized this abnormal hemoglobin, named "hemoglobin Hôtel-Dieu". An important associated smoking habit, probably responsible of an abnormal lung X-ray and of a disturbed CO transport, contributed to increase the difficulty of diagnosis. Familial inquiry, the search of an abnormal hemoglobin by standard or isoelectrofocusing electrophoresis, and the 2,3-DPG assay should be systematically performed in case of polycythemia in young people or in the absence of obvious aetiology. A corpuscular abnormality can be thus detected in about 10 p. cent of such polycythemias.

Adult↗
PubMed1978

Hemoglobin Hoshida (beta43 (cd-2) Glu leads to Gln), a new hemoglobin variant discovered in Japan.

An electrophoretically G-like hemoglobin variant, Hb Hoshida, was detected from a ten year old girl and her mother. No clinical and hematological abnormalities were seen in the individuals heterozygous for this mutant gene. Structural studies of this abnormal hemoglobin demonstrated a previously undescribed substitution of beta43 (CD-2) Glu leads to Gln. The proportion of the abnormal hemoglobin in hemolysate was 42.1 per cent. The hemoglobin revealed neither instabilities nor functional abnormalities.

Child↗
PubMed1998

Access to a syllabus of human hemoglobin variants (1996) via the World Wide Web.

Information on mutations in human hemoglobin is important in many efforts, including understanding the pathophysiology of hemoglobin diseases, developing therapies, elucidating the dynamics of sequence alterations inhuman populations, and dissecting the details of protein structure/function relationships. Currently, information is available on a large number of mutations and variants, but is distributed among thousands of papers. In an effort to organize this voluminous data set, two Syllabi have been prepared compiling succinct information on human hemoglobin abnormalities. In both of these, each entry provides amino acid and/or DNA sequence alterations, hematological and clinical data, methodology used for characterization, ethnic distribution, and functional properties and stability of the hemoglobin, together with appropriate literature references. A Syllabus of Human Hemoglobin Variants (1996) describes 693 abnormal hemoglobins resulting from alterations in the alpha-, beta-, gamma-, and delta-globin chains, including special abnormalities such as double mutations, hybrid chains, elongated chains, deletions, and insertions. We have converted this resource to an electronic form that is accessible via the World Wide Web at the Globin Gene Server (http://globin.cse.psu.edu). Hyperlinks are provided from each entry in the tables of variants to the corresponding full description. In addition, a simple query interface allows the user to find all entries containing a designated word or phrase. We are in the process of converting A Syllabus of Thalassemia Mutations (1997) to a similar electronic format.

Computer Communication Networks↗
PubMed1985

Pregnancy in carriers of high-affinity hemoglobins.

Pregnancy in female carriers of abnormal hemoglobins with great avidity for oxygen provides a unique opportunity to assess the importance of the usual difference in oxygen affinity between fetal and maternal blood. Outcome of pregnancy was recorded for carriers of hemoglobins Bethesda, Osler, and Yakima, whose p50s (9.5, 9.1, and 12 mm Hg at pH 7.4) were far lower than that of a normal fetus (23 mm Hg at pH 7.3). Neither spontaneous abortions nor intrauterine growth retardation could be attributed to the presence of high oxygen affinity in the mothers. In vitro simulations suggested that neither maternal or fetal polycythemia alone was sufficient to adjust for perturbation of the normal situation, and increased uterine and/or fetal blood flow probably provided additional compensation.

Adult↗
PubMed1981

High performance liquid chromatography in the identification of human hemoglobin variants.

A description is given of the nature of column packings for reverse phase high performance liquid chromatography (HPLC) and of the equipment that is available for HPLC procedures. HPLC methods have been applied to the identification of abnormal hemoglobins. In most instances, the variant peptide(s) is easily detected on the chromatogram. The effect of differences in column packings and developer sequences is described; modifications in either provide many means for achieving desired separations. Thus, HPLC separates peptides well and is a rapid, sensitive method for studying hemoglobin. Although the emphasis has been on the examination of peptides of abnormal hemoglobins, the procedure can be extended to other aspects such as the separation of hemoglobin chains themselves.

Chromatography, High Pressure Liquid↗
PubMedDate not supplied

[Hemoglobin J. Broussais alpha-2 90 Lys leads to Asn beta-2A (FG2) discovered in a Martinique family. Comparison of several analytical technics].

We report a new case of hemoglobin J. Broussais, present in its heterozygote form in a seven year old child from Martinque. The structural characteristics of this abnormal hemoglobin have been compared by three methods: 1. By analytical and preparative finger-printing on silica gel thin layer plates after tryptic digestion. 2. By a programmed separation of tryptic peptides on various ion exchange resins. 3. And by automatic sequencing of the peptides obtained following CNBr cleavage and separation by gel filtration chromatography. The functional behaviour of this hemoglobin was not modified by the substitution of an Asn for a Lys residue at position 90, although its presence induced slight hematological disorders in the patient. Abnormal hemoglobins which have been identified in Martinique and Guadeloupe are reviewed.

Amino Acid Sequence↗
PubMed1982

Homozygous alpha thalassemia/Hb G Philadelphia.

Microcytic red cells from a 70 year old Negro man with mild anemia contained only hemoglobin G-Philadelphia. Red cells from all of his children had low-normal MCV's, and contained 32-34 percent of the abnormal hemoglobin. Oxygen affinity of his blood and stability of his hemolysate were normal, suggesting that his mild anemia was not caused by the the abnormal hemoglobin. Restriction endonuclease analyses of DNA from the proband and his offspring showed that the alpha G-Philadelphia globin gene exists in only one copy per chromosome. The new gene was probably created by an unequal cross-over which deleted an alpha globin coding sequence (derived from one or both alpha globin genes), as well as some or all of the DNA sequence between those genes.

Aged↗
PubMed2004

[Hemoglobin Korle-Bu [beta73(E17)Asp ->Asn]. First cases described in Spain].

BACKGROUND AND OBJECTIVE: Hemoblobin Korle-Bu [beta73(E17)Asp->Asn], also known as hemoglobin GACCRA, is frequent in African colour population. The interest of this work has been confirmed that hemoglobin Korle-Bu is a structural variant which mutation is located in the CD73 (GAT->AAT) of the exon 2 of beta gene and that this characterises has been made in the first cases found in Spanish population. Where to be carrier of African hemoglobins is less frequent. PATIENTS AND METHOD: Two unrelated families (4 subjects) from the same geographical area were studied because all of them shown an abnormal hemoglobin during a screening program of hemoglobinopathies in blood donors. Electrophoretic methods and ion exchange HPLC studied this hemoglobin. Globin chains are studied by reverse phase HPLC. Automatic sequencing carried out the molecular study. RESULTS: In the electrophoretic study and by ion exchange HPLC was observed an abnormal hemoglobin. The study of globin chains by reverse phase HPLC revealed the presence of three peaks betaX, betaA y alpha. In all the cases, the P50 was increased. The molecular study by sequencing revealed the substitution GAT->AAT in the codon 73 of beta gene globin. This variant of haemoglobin is named hemoglobin Korle-Bu [beta73(E17)Asp->Asn]. CONCLUSIONS: This hemoglobin variant becomes important when it is associated with hemoglobin S or C because, although it is not associated with a clinical picture severe, when this hemoglobin is associated with another kind of alterations of hemoglobin molecule (thalassemias or hemoglobinopathies) the clinical could be more severe. So, it is important its genetic characterization for the diagnoses of the serious forms.

Female↗
PubMed1974

Hemoglobinopathic erythrocytosis due to a new electrophoretically silent variant, hemoglobin San Diego (beta109 (G11)val--met).

Examination of 13 members of a Filipino family revealed that 6 had erythrocytosis inherited as a simple autosomal dominant trait. Application of several electrophoretic and chromatographic tests failed to reveal the presence of an abnormal hemoglobin in hemolysates from affected individuals. However, measurements of oxygen dissociation curves using whole bloods, dialyzed hemolysates, and 2,3-diphosphoglyceric acid-stripped hemolysates clearly showed that affected persons had an abnormal hemoglobin characterized by a high affinity for oxygen. Compositional analyses of all tryptic peptides from the beta-chains of the proband revealed a valyl-methionyl ambiguity in betaT12a. Blockage of lysyl residues and subsequent tryptic hydrolysis at arginyl residues permitted the isolation of fragments containing residues 105 through 146. Automatic sequence analysis of the fragments demonstrated the presence of both valine and methionine in nearly equal proportions at position beta109. This new hemoglobin variant is designated Hb San Diego (beta109(G11) Val-->Met).

Adolescent↗
PubMed1977

Hemoglobin Tak in a newborn Malay.

The trait condition for hemoglobin Tak, was found in a 4-day old newborn Malay who suffered from severe neonatal jaundice. The beta chain of the abnormal hemoglobin was elongated by 11 residues at the C-terminus and had the same structure as reported for Hb Tak. The mother was heterozygous for this abnormal hemoglobin, the father was normal. The mother and child, 4 years later, did not show clinical or hematological symptoms except definitely increased resistance of their erythrocytes to hypotonic saline solutions and slight anisopoikilocytosis. The abnormal gene in the two reported Thai families and in our Malay family may have the same origin.

Hemoglobins, Abnormal↗
PubMed1983

Relation between variations in the phenotypic expression of an unstable hemoglobin disorder (hemoglobin Zürich) and carboxyhemoglobin levels.

Longitudinal studies in a group of 15 asymptomatic subjects with hemoglobin Zürich from two unrelated families indicated marked variation in the clinical and hematologic expression of the hemoglobinopathy, even within the same family. Carbon monoxide bound to normal hemoglobin stabilized the molecule when exposed to a variety of denaturing procedures. The marked increase in the affinity of hemoglobin Zürich for carbon monoxide, approximately 65 times that of normal hemoglobin, led to a study of carboxyhemoglobin levels in smoking and nonsmoking subjects with hemoglobin Zürich and their relation to the phenotypic expression of the hemoglobinopathy. The carboxyhemoglobin content in whole blood from persons with hemoglobin Zürich ranged from 3.9 to 6.7 percent in nine nonsmokers and from 9.8 to 19.7 percent in six smokers. Rates of hemolysis as determined by values for hematocrit, reticulocyte count, and haptoglobin and hemopexin levels were less in smokers than in nonsmokers. Also, rates of Heinz body formation in intact red cells and isopropanol-induced precipitation of the abnormal hemoglobin in hemolysates were less in smokers than in non-smokers. These observations suggest that variability in the phenotypic expression of hemoglobin Zürich is a post-translation event secondary to stabilization of the abnormal hemoglobin by carbon monoxide.

Adolescent↗
PubMedDate not supplied

[Location of amino acid substitutions in human hemoglobin. Mass spectrometric rapid analysis of tryptic peptides].

Point mutations alpha 58 His----Tyr (Hb M Boston), beta 6 Glu--lys (Hb C) and beta 26 Glu----Lys (Hb E) have been identified in abnormal hemoglobins by means of tryptic hydrolysis of their alpha- and beta-chains followed by mass-spectrometry coupled with direct extraction of ions from solution. The abnormal hemoglobin Hb M Boston alpha 58 (E7) His----Tyr has been for the first time found in the blood of a patient from the USSR. This express-method is generally applicable for the identification of point mutation in proteins. The amount of protein necessary for the analysis is 100-1000 pmole. The stability, proteolytic degradation of the identified abnormal Hb's and Hb Bart's were investigated. The molecular pathogenesis of the hemoglobinopathies are discussed from the point of view of the observed properties.

Amino Acids↗
PubMed2003

[A variant hemoglobin found by dissociation of blood glucose from HbA1c on routine physical examination].

Discrepancy between HbA1c measured by routine HPLC and blood glucose was observed in four out of 340 persons on physical examination. We investigated whether this discrepancy was due to abnormal hemoglobin. HbA1c was measured by routine HPLC and latex agglutination. For further examinations, a hemoglobin specimen was analyzed by weak cation-exchange column(PolyCAT A) chromatography, ESI/MS and MS/MS. HbA1c levels measured by HPLC were about half of those measured by latex agglutination. An abnormal peak between HbA1c and HbA0 was detected on HPLC chromatography in three consanguineous persons. The abnormal hemoglobin from one of the related person was also confirmed by PolyCAT A chromatography. The hemoglobin specimen contained almost same amounts of normal HbA0 and abnormal Hb. Analyses of the globin by ESI/MS and MS/MS revealed that glutamate at the 22nd amino acid residue of the beta-chain was replaced by alanine. This variant was the same as HbG-Coushatta[beta 22(B4) Glu-->Ala]. Family studies showed that the variant was inherited as a dominant trait. The dissociation observed in the case was due to a presence of a variant hemoglobin. In the other case HbA1c levels measured by the two methods were similarly low, and no abnormal peak was observed on HPLC chromatography. Similar studies on the hemoglobin of this case did not disclose any abnormalities. The low values of HbA1c of this case were considered in the lowest region of the normal range.

Aged↗