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PubMedDate not supplied

Hemoglobin Willamette (alpha2beta2 51Pro replaced by Apg (D2)) a new abnormal human hemoglobin.

A hemoglobin variant with the same electrophoretic mobility as hemoglobin S was found in three generations of a black family. No clinical symptoms or findings were present in subjects heterozygous for this mutant. Except for target forms of mature erythrocytes, they have no abnormal hematologic findings. Structural studies demonstrated a previously undescribed substitution, beta51 Pro replaced by Arg, in the abnormal fraction which accounts for about one-third of the total hemoglobin. This fraction is more unstable in vitro at 65 degrees than normal A hemoglobin. Both whole blood and purified abnormal hemoglobin have increased oxygen affinity and a slightly decreased Bohr effect.

Arginine↗
PubMed1988

[Micropreparative thin-layer peptide maps in the molecular diagnosis of abnormal human hemoglobins].

General factors determining the possibility of application of peptide maps in thin layer of microcrystalline cellulose as a micropreparative method in molecular diagnostics of abnormal hemoglobins were studied. The effects of absorbtional capacity of cellulose and amino acid impurities in it, choice of eluent and elution technique, peptide structure and extent of its modification in staining as well as completeness and specificity of globin chain enzymatic digestion on peptides extraction from thin layer were analysed. The results of structural identification of Hb D Punjab beta 121 Glu----Gln at a Cypriot; Hb O Arab; beta 121 Glu----Lys at a Bulgarian woman, living in Kalinin region (the second case in the USSR); Hb M Saskatoon beta 63 His----Tyr at a woman from Georgia (the second case in the USSR); Hb Buenos Aires beta 85 Phe----Ser at a Russian girl (the first case in the USSR and the third case in the world); Hb Dagestan alpha 60 Lys----Glu at two members of a Lesgin family from Dagestan; Hb Agenogi beta 90 Glu----Lys at a Hungarian woman; Hb Setif alpha 94 Asp----Tyr at three patients from Cyprus and Hb Detroit beta 95 Lys----Asn at an Azerbaijanian woman (the first case in the USSR and the second case in the world) are presented.

Amino Acids↗
PubMed1988

[A new strategy for structural identification of abnormal human hemoglobins].

A new strategy for structural identification of abnormal human hemoglobins is proposed. It is based on micropreparative modification of electrophoretic separation of globins on Cellogel strips with subsequent quantitative isolation of a pure, desalted globin chain, in a form suitable for its subsequent structural investigation. Among the major advantages of the new strategy age possibility to use small blood samples (0.1-0.2 ml), short analysis time, relative simplicity and low cost.

Blood Protein Electrophoresis↗
PubMed1981

Hemoglobin bologna (alpha 2 beta 2 61 (E5) lys replaced by met). An abnormal human hemoglobin with low oxygen affinity.

An abnormal human hemoglobin was found in association with beta-thalassemia in a hemolysate from an 11-year-old healthy child living in Bologna (northern Italy). Structural studies demonstrated a previously unreported amino acid substitution, beta 61 (E5) Lys replaced by Met (this is an external residue). The new variant has been named Hb Bologna, and is characterized by a reduced oxygen affinity. Family studies indicated that the variant had been inherited from the father, a 41-year-old male of Southern Italian origin. Also, a brother of the propositus was found to be an abnormal Hb carrier.

Adult↗
PubMed1978

Hemoglobin Legnano (alpha2 141 (HC3) Arg replaced by Leu beta2): a new abnormal human hemoglobin with high oxygen affinity.

An abnormal, fast moving hemoglobin was noted in a 34-yr-old male patient living in Legnano (northern Italy) affected with renal failure and iron deficiency anemia, not related to the presence of the Hb variant. Structural studies have demonstrated a previously undescribed amino acid substitution, alpha 141 Arg replaced by Leu. This new variant has been named Hb Legnano, and is characterized by an increased oxygen affinity and a low cooperativity, at least as far as preliminary functional studies carried out on whole blood have indicated. Family studies are reported: three other heterozygous carriers were observed among the relatives of the propositus, all showing a mild polycythemia which, however, does not seem to produce appreciable clinical consequences.

Adult↗
PubMedDate not supplied

[Retina and qualitative abnormalities of hemoglobin (author's transl)].

The classification of the main qualitative abnormalities of hemoglobin is recalled. The five phases of the retinal changes caused by drepanocytosis are described. Their pathogenesis is explained. The specialized treatment is photocoagulation after cryokiming coagulation has been discarded. Nowadays laser is used but the timing and the indications for this treatment are not yet fixed.

Fluorescein Angiography↗
PubMed1983

Effect of chloride ion on the oxygen affinity of hemoglobin York (alpha 2 beta 2(146)Pro) and S-York hybrid hemoglobin (alpha 2 beta S beta York). Role of the beta 82 lysyl and beta 146 histydyl residues in chloride binding to hemoglobin.

We estimated the relative role of various chloride binding sites in determining the oxygen affinity of hemoglobin using abnormal hemoglobins such as Hb York (Hb Y) (alpha 2 beta 2(146)Pro), Hb Malmö (Hb M) (alpha 2 beta 2(97)Gln), and Hb S and chemically modified hemoglobins such as cross-linked Hb S, Hb Y, and asymmetrical SY hemoglobin with bis(3,5-dibromosalicyl)fumarate. The chloride effect on the p50 values of Hb S and Hb M was identical to that of Hb A. In contrast, the effect of chloride on the p50 values of Hb Y was only 20% of that of Hb A. Cross-linking between the two beta 82 lysyl residues with fumarate decreased the chloride effect by 40%. The effect of chloride on cross-linked Hb Y, in which both beta 82 lysyl and beta 146 histidyl residues were modified, was unchanged from that on Hb Y (20% of Hb A). The effect of chloride on the p50 value of SY asymmetrical hybrid hemoglobin was 40% of that of Hb A or Hb S, which is midway between the values obtained for cross-linked Hb S and Hb Y. From these results, the contribution of beta 146 His and beta 82 Lys on oxygen affinity by binding of chloride was calculated to be 40% each; the remaining 20% chloride effect was attributed to alpha 1 Val.

Chlorides↗
PubMed1988

Micropreparative electrophoresis of globin chains on cellulose acetate film in structural identification of abnormal human hemoglobins.

A simple and rapid micropreparative method for isolating 5 to 30 nmol of globin chain, followed by structural identification of abnormal human hemoglobins, is described. The method is based on the electrophoretic separation of globins on ordinary Cellogel films under denaturating conditions with subsequent cutting out of the protein zones and solubilization of Cellogel and the electrophoretic buffer components in a specially selected solvent in which the globin chain undergoes quantitative precipitation. The method makes it possible to simplify and speed up the structural identification of commonly occurring abnormal hemoglobins. The advantages and limitations of the method are discussed along with its potential uses in structural protein chemistry.

Cellulose↗
PubMed1969

Hemoglobin Philly (beta 35 tyrosine phenylalanine): studies in the molecular pathology of hemoglobin.

An abnormal unstable hemoglobin, hemoglobin Philly, was found in three members of a family, each of whom had evidence of a chronic hemolytic state. The presence of the mutant protein was suggested by the rapid appearance of inclusion bodies upon incubation of erythrocytes with brilliant cresyl blue and by the increased heat precipitability of the hemoglobin. However, no abnormal hemoglobin could be demonstrated by electrophoresis or column chromatography. Sulfhydryl titration of the hemolysates with p-mercuribenzoate indicated that there was an average of four reactive sulfhydryl groups per hemoglobin molecule instead of the usual two. The total number of hemoglobin sulfhydryl groups was normal; six groups were measured when denatured globin was reacted with 5,5'-dithiobis[2-nitrobenzoic acid]. This indicated that the increased sulfhydryl reactivity was due to an increased availability to p-mercuribenzoate of the usually unreactive hemoglobin cysteines at beta112 and alpha104. After treatment for (1/2) hr with 4-5 moles of p-mercuribenzoate per mole of hemoglobin, electrophoresis revealed that 30-35% of the hemoglobin had been dissociated into alpha- and beta-chains. Normal hemolysates revealed negligible splitting after 72 hr of similar treatment. The alpha- and beta-chains of hemoglobin Philly were separated from the unsplit hemoglobin A by carboxymethyl cellulose chromatography. Fingerprint and amino acid analyses revealed that tyrosine beta35 was replaced by phenylalanine. In hemoglobin Philly there is loss of the normal hydrogen bond between the tyrosine hydroxyl group and the carboxyl group of aspartic acid alpha126 at the alpha(1)beta(1) contact. This shifts the equilibrium from hemoglobin tetramers toward monomers, exposing the beta112 and alpha104 cysteines. In the cell, precipitation of the unstable monomers may contribute to erythrocyte destruction.

Amino Acids↗
PubMed2005

[Associated factors to abnormal glucosylated hemoglobin in the postpartum period].

OBJECTIVE: To demonstrate the association between risk factors and abnormal glucosylated hemoglobin detected in women during the postpartum period. PATIENTS AND METHODS: A case and control study was carried out at the Hospital Civil de Guadalajara Dr. Juan I. Menchaca during six months. Glucosylated hemoglobin and glucose concentration from 160 fasting women with a pregnancy > or =28 weeks was obtained during the postpartum period. With an odds ratio and confidence interval (95%) the epidemiological meaning of risk factors was identified. RESULTS: The abnormal glucosylated hemoglobin was significantly associated to: single, separated and divorced women (p < 0.05); major frequency of previous caesarean (OR: 2.78, IC 95%:1.25-6.22), p = 0.006, and higher proportion of children with congenital malformations (OR: 12, IC 95%: 1.38-104), p = 0.01. In the group cases 48% of caesareans was associated to probable gestational diabetes: moderate preeclampsia, eclampsia, fetal macrosomy, and preterm deliveries. CONCLUSION: It is necessary to make an early detection of risk factors associated to abnormal glucosylated hemoglobin and to prevent adverse effects as congenital malformations and clinical complications that increase the incidence of caesarean.

Adult↗
PubMed1976

Hemoglobin Vancouver [alpha2beta2(73)(E17) Asp replaced by Tyr]: its structure and function.

Hemoglobin Vancouver is a new abnormal hemoglobin with an amino acid substitution of the normal aspartyl residue 73 of the beta chain by a tyrosyl residue. It was discovered in a man of Chinese descent in association with beta thalassemia. It was subsequently detected in a sister in association with normal Hb A. The oxygen affinity of the abnormal hemoglobin is decreased but its subunit interaction is normal. The Bohr effect may be slightly increased. This is the fourth abnormal hemoglobin to be found with a substitution at beta73. The others are Hb C-Harlem (alpha2beta2 6Glu replaced by Val and 73 Asp replaced by Asn), Hb Korle-Bu (alpha2beta2 73Asp replaced by Asn), and Hb Mobile (alpha2beta2 73Asp replaced by Val). Although Hb Mobile was found in the present studies to have a decreased affinity for oxygen, Hbs C-Harlem and Korle-Bu have been reported to be normal. These observations of functional differences for variants of beta73 added to earlier observations of the role of the normal beta73 residue to the aggregation of sickle deoxyhemoglobin indicate that this position of the molecule may be important in intra as well as intermolecular interactions.

Amino Acid Sequence↗