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At least 19 recordsLinked to original sources
PubMed1981

Hemoglobins, XLI. The embryonic hemoglobins of mammal. A new hemoglobin, hemoglobin Heide II (Hb HeII: alpha 2 epsilon 2), and demonstration of the hemoglobin structure of gower I (zeta 3 epsilon 2) in the pig embryo.

A new hemoglobin is described. The hemoglobins of pig embryonic erythrocytes are separated by DEAE-Cephacel chromatography. In addition to a small amount of adult hemoglobin, four embryonic hemoglobins are obtained. Each of the hemoglobin components is analysed by globin and hemoglobin electrophoresis on polyacrylamide gels. Two of these hemoglobins are previously described as Hb Gower II (alpha 2 epsilon 2) and Heide I (zeta 2 epsilon 2). A tetrameric hemoglobin consisting of alpha and epsilon chains has been detected. Therefore, this new hemoglobin is named, in analogy, as Hb Heide II (alpha 2 epsilon 2). Furthermore, the other hemoglobin tetramer has been unequivocally identified as zeta 2 epsilon 2. This structure corresponds to Gower I which is only suggested in the human embryo.

Animals↗
PubMed2002

The novel HemoCu plasma/low hemoglobin system accurately measures small concentrations of three different hemoglobin-based oxygen carriers in plasma: hemoglobin glutamer-200 (bovine) (Oxyglobin), hemoglobin glutamer-250 (bovine) (Hemopure), and hemoglobin-Raffimer (Hemolink).

UNLABELLED: The accuracy of the HemoCue Plasma/Low Hemoglobin System was validated in vitr. with low levels of hemoglobin-based oxygen carriers (HBOCs). Repeated measurements were performed on 50 samples of canine plasma, each mixed with three different HBOCs at varying small concentrations (a total of 150 samples), by using plasma samples without HBOCs as controls. Two technicians performed the measurements and randomly tested each sample 10 times. The results were analyzed for correlation, and analysis of variance was used to evaluate statistical significance, with a P value of </=0.05 considered significant. Hemoglobin concentrations determined with the bedside photometer were not significantly different from known values of hemoglobin concentration in the samples. There was no significant difference between values obtained by two independent observers for the same samples. This was true for all three tested HBOCs and for all tested concentrations. The mean bias of the measurement expressed as a percentage of sample concentration was 0.1% for hemoglobin glutamer-200 (bovine), 0.58% for hemoglobin glutamer-250 (bovine), and 0.19% for hemoglobin-raffimer. The mean error was <8% for all three HBOCs. Both intraobserver and interobserver reliabilities were high and statistically significant. The HemoCue Plasma/Low Hemoglobin System is a reliable instrument for detecting and measuring small concentrations of three different HBOCs in plasma. IMPLICATIONS: This study evaluated a new bedside blood-measuring device for low levels and found that it rapidly measured low levels accurately for three blood substitutes.

Air↗
PubMed2002

Flow cytometric measurement of hemoglobin F in RBCs: diagnostic usefulness in the distinction of hereditary persistence of fetal hemoglobin (HPFH) and hemoglobin S-hPFH from other conditions with elevated levels of hemoglobin F.

The cellular distribution of hemoglobin F is important for evaluating persistently elevated hemoglobin F levels, such as in hereditary persistence of fetal hemoglobin (HPFH) or delta/beta-thalassemia, and for differentiating homozygous hemoglobin S (or hemoglobin S-beta(0)-thalassemia) from hemoglobin S-HPFH, traditionally done by using the Kleihauer-Betke (K-B) acid elution test. We evaluated a flow cytometric method using an anti-hemoglobin F antibody as a replacement for the K-B test. We used 172 specimens representing a variety of conditions: HPFH trait, 19 cases; delta/beta-thalassemia trait, 8 cases; hemoglobin S-HPFH, 10 cases. By flow cytometry, all cases of HPFH trait gave a hemoglobin F pattern comparable to the homocellular pattern obtained by the K-B test; all cases of delta/beta-thalassemia tested gave a pattern comparable to a K-B heterocellular pattern. Most cases of hemoglobin S-HPFH gave a homocellular distribution of hemoglobin F whereas all cases of homozygous hemoglobin S with elevated hemoglobin F levels gave a heterocellular pattern. Flow cytometry provides a more rapid and objective method for assessing cellular distribution of hemoglobin F and is useful for patient evaluation when HPFH trait, delta/beta-thalassemia trait, or hemoglobin S-HPFH trait is suspected.

Adult↗
PubMed1993

The determination of absorption coefficients for measurement of carboxy-hemoglobin, oxy-hemoglobin, reduced hemoglobin, and met-hemoglobin in sheep using the IL482 CO-Oximeter.

The IL482 CO-Oximeter uses four wavelengths of visible light to analyze blood samples for the relative percentages of oxy-, carboxy-, reduced, and met-hemoglobin. In the analysis, the absorption at each of the wavelengths is multiplied by a matrix of four coefficients to derive the quantities of the four hemoglobin types. The normal settings of the CO-Oximeter coefficients are those for adult human hemoglobin. However, animal blood can be measured provided that the appropriate matrix of coefficients is available. Instrumentation Laboratory has provided sets of coefficients for several animal species. The company has also published a protocol for determining coefficients for other animal species. This protocol was examined using sheep hemoglobin-A blood and found to be inaccurate. The IL482 protocol is unsatisfactory because, if the initial error is large, successive iterations to determine the coefficient matrix through revision of the estimates of residual hemoglobin types do not converge. With sheep type-A hemoglobin, the use of human coefficients for the initial estimate gave a value of 6%, whereas, by chromatography, the carboxyhemoglobin (COHb) was 0.12% (i.e., a better initial estimate would be zero). When this was done, the final COHb estimate on "as-drawn" blood was within 1% of the COHb measured independently by gas chromatography. Revision of the protocol gave a markedly better accuracy, within 2% for COHb over the whole range when tested against mixtures of CO and O2 tonometered blood.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1987

Specifically carboxymethylated hemoglobin as an analogue of carbamino hemoglobin. Solution and X-ray studies of carboxymethylated hemoglobin and X-ray studies of carbamino hemoglobin.

Hemoglobin can be specifically carboxymethylated at its NH2-terminal amino groups (i.e. HbNHCH2COO-) to form the derivatives alpha 2Cm beta 2, alpha 2 beta 2Cm, and alpha 2Cm beta 2Cm, where Cm represents carboxymethyl. Previous studies (DiDonato, A., Fantl, W. J., Acharya, A. S., and Manning, J. M. (1983) J. Biol. Chem. 258, 11890-11895) suggested that these derivatives could be used as stable analogues of the corresponding carbamino (Hb-NHCOO-) forms of hemoglobin, adducts that are generated reversibly in vivo when CO2 combines with alpha-amino groups. In this paper we present x-ray diffraction studies of both carbamino hemoglobin and carboxymethylated hemoglobin that verify this proposal and we use the carboxymethylated derivatives to study the functional consequences of placing a covalently bound carboxyl group at the NH2 terminus of each hemoglobin subunit. Our studies also provide additional information concerning the oxygen-linked binding of anions and protons to Val-1 alpha. Difference electron density analysis of deoxy alpha 2Cm beta 2Cm versus the unmodified deoxyhemoglobin tetramer (deoxy alpha 2 beta 2) shows that the covalently bound carboxyl moieties replace inorganic anions that are normally bound to the free NH2-terminal amino groups in crystals of native deoxyhemoglobin grown from solutions of concentrated (2.3 M) ammonium sulfate. In the case of the beta-subunits, the carboxymethyl group replaces an inorganic anion normally bound between the alpha-amino group of Val-1 beta, the epsilon-amino group of Lys-82 beta, and backbone NH groups at the NH2-terminal end of the F'-helix. In the case of the alpha-subunits, the carboxymethyl group replaces an anion that is normally bound between the alpha-amino group of Val-1 alpha and the beta-OH group of Ser-131 alpha. A corresponding difference electron map of carbamino deoxyhemoglobin in low-salt (50 mM KCl) crystals shows that CO2 bound in the form of carbamate occupies the same two anion binding sites. The alkaline Bohr effect of alpha 2Cm beta 2 is only marginally lower (approximately 7%) than that of alpha 2 beta 2. Previous studies (Kilmartin, J. V., 1977) have shown that about 30% of the alkaline Bohr effect is the result of an oxygen-linked change in the pK alpha of Val-1 alpha, and O'Donnell et al., 1979, found that this portion of the Bohr effect is the result of the oxygen-linked binding of chloride to Val-1 alpha.(ABSTRACT TRUNCATED AT 400 WORDS)

Binding, Competitive↗
PubMed1977

The hemoglobins of Artemia salina. IV. A model for genetic control of hemoglobin 1, hemoglobin 2, and hemoglobin X.

Two loci account for all genetic variation resulting in difference in electrophoretic mobility in three hemoglobins (Hb1, Hb2, and HbX) in the hemolymph of the brine shrimp. Four alpha alleles and nine beta alleles have been studied. In shrimps of all genotypes and in electrophoresis in media with varying degrees of molecular sieving, Hb2 is approximately equidistant from Hb1 and HbX. A shrimp heterozygous at both loci has a three-banded Hb1, a four-banded Hb2, and a three-banded BbX. We conclude that Hb2 contains n alpha-polypeptides and n beta-polypeptides. Hb1 contains 2n alpha-polypeptides. HbX contains 2n beta-polypeptides. During electrophoresis, the three native hemoglobins undergo reversible dissociation to n subunits. Subunits with the same charge reassemble to migrate as molecules of the same size as the native molecules. Although there is no evidence for an additional polypeptide in the three hemoglobins, we cannot exclude such a possibility. If it exists, it is under three constraints: (1) it must be present in equal amounts in each of the three hemoglobins; (2) it must have the same molecular weight as the alpha- and beta-polypeptides; and (3) it must be free of genetic variation (detectable by electrophoresis).

Alleles↗
PubMed1987

Fetal hemoglobin-containing cells have the same mean corpuscular hemoglobin as cells without fetal hemoglobin: a reciprocal relationship between gamma- and beta-globin gene expression in normal subjects and in those with high fetal hemoglobin production.

We have developed methodology that allows comparison of the mean corpuscular hemoglobin (MCH) of fetal hemoglobin (HbF)-containing red cells (F cells) with the MCH of non-F cells from the same individual. To do this, suspensions of peripheral blood erythrocytes and their internal contents are fixed with an imidodiester, dimethyl-3,3'-dithiobispropionimidate dihydrochloride (DTBP). Thereafter fixed cells are made permeable to antisera by treatment with Triton X-100 and isopropanol, reacted with a mouse monoclonal antibody (MoAb) against HbF, and then with fluorescein-conjugated antimouse IgG. No appreciable hemoglobin is lost during such manipulation. Red cells from a diversity of subjects were thus treated and examined microscopically, first by transmitted light and then by epifluorescence. A direct correlation between Coulter-derived MCH and mean absorbance of 415 nm transmitted light was found for 100 unfixed (r = 0.96) and for 100 antibody-treated fixed-permeabilized red cells (r = 0.99) among individuals selected so as to provide a range of Coulter MCH values between 20 and 35. Comparisons of microscopically derived MCH of F cells and non-F cells were statistically nondistinguishable (P greater than 0.05) in all subjects. Such comparisons included normal individuals (less than 1% F cells), SS patients (7% to 48% F cells), subjects with congenital anemia (22% to 65% F cells), individuals with heterocellular hereditary persistence of HbF (HPFH) (12% to 21% F cells), and heterozygotes for beta + thalassemia (11% to 31% F cells). We conclude that gamma- and beta-globin production within F cells is regulated in a reciprocal fashion both among normal individuals and among individuals with elevated HbF production.

Anemia↗
PubMed2002

The HemoCue, a point of care B-hemoglobin photometer, measures hemoglobin concentrations accurately when mixed in vitro with canine plasma and three hemoglobin-based oxygen carriers (HBOC).

PURPOSE: Accuracy of measurement of low hemoglobin concentrations using the HemoCue, a B-hemoglobin photometer (HemoCue AB, Angelholm, Sweden) may exhibit significant variability. Infusion of hemoglobin-based oxygen carriers (HBOC) results in low concentrations of plasma hemoglobin. Our study assessed B-hemoglobin photometer measurement accuracy of three HBOC: (hemoglobin glutamer-200 (bovine; Oxyglobin, Biopure Corp., Cambridge, MA, USA); hemoglobin glutamer-250 (bovine; Hemopure, Biopure Corp, Cambridge, MA, USA), and hemoglobin-raffimer, (human; Hemolink, Hemosol, Inc., Toronto, Ontario, Canada). METHODS: In the laboratory, 45 split canine plasma samples were mixed with hemoglobin glutamer-200 (8.13, 16.25, 32.5 g x L(-1) concentrations), 45 samples were mixed with hemoglobin glutamer-250 (8.13, 16.25, 32.5 g x L(-1) concentrations), 45 with hemoglobin-raffimer (12.5, 25.0, 50.0 g x L(-1) concentrations), and measured. Plasma samples without HBOC served as control. Hemoglobin concentration was determined by a laboratory analyzer (Coulter Corporation, Hiafeah, FL, USA) and B-hemoglobin photometer (HemoCue, Angelholm, Sweden). Two independent technicians performed blinded sample measurements and randomly tested each sample five times. Results were analyzed according to Bland and Altman analysis. RESULTS: B-hemoglobin photometer demonstrated high repeatability for all three HBOCs. Repeatability coefficients were 0.37 g x L(-1) and 0.48 g x L(-1) for hemoglobin glutamer-200, 0.39 g x L(-1) and 0.4 g x L(-1) for hemoglobin glutamer-250 and 1.07 g x L(-1) and 0.85 g x L(-1) for hemoglobin-raffimer. An acceptable agreement was found between the B-hemoglobin photometer and the laboratory analyzer for all three HBOCs tested. CONCLUSION: The B-hemoglobin photometer accurately determined the concentration of three HBOC solutions dissolved in canine plasma.

Animals↗
PubMed1986

Densitometry and microchromatography compared for determination of the hemoglobin C and A2 proportions in hemoglobin C and hemoglobin SC disease and in hemoglobin C trait.

Using both densitometry and anion-exchange microchromatography, we measured hemoglobin C (Hb C) and Hb A2 proportions in 11 patients, eight of whom had Hb AC, two Hb SC, and one Hb CC. For one patient with Hb SC, we made the determinations before and after a transfusion. The mean (and SD) for the sum of Hb C + Hb A2 by densitometry and anion-exchange microchromatography for the nine patients with Hb AC and Hb CC were 45 (18) and 40 (18)%, respectively (p greater than 0.1, r = 0.98); for the three determinations involving the two Hb SC patients, the respective proportions were 40 (9.9) and 38 (6.6)% (r = 0.88). Electrophoretic analysis of microchromatographic eluates from the Hb AC and Hb CC patients showed that 6% of the absorbance of the late high-ionic-strength eluate was due to Hb C, which was responsible for the statistically insignificant difference between densitometric and chromatographic values for Hb C + A2 values. Electrophoresis on cellulose acetate of concentrated eluates of the Hb C + A2 fraction from the two Hb SC patients revealed no contamination by Hb S. Evidently, microchromatography can be used to determine Hb C + A2 in patients with Hb C or Hb SC disease or Hb C trait.

Anemia, Sickle Cell↗
PubMed1977

The hemoglobins of Artemia salina. V. Genetic variation in hemoglobin 1, hemoglobin 2, and hemoglobin 3.

Electrophoretic mobilities of three hemoglobins (Hb1, Hb2, and Hb3) were studied in 15 populations of brine shrimps. Genetic segregation data support the model that Hb2 contains n alpha-polypeptides and n beta-polypeptides; Hb1 contains 2n alpha-polypeptides- Hb3 contains neither alpha- nor beta-polypeptides. There is no evidence of linkage of alpha and beta loci with each other or with the locus (or loci) which governs Hb3 or with the nonhomologous portion of the sex chromosomes. Hemoglobins of different populations may be hybridized in vitro by incubation at high temperature. Reversible dissociation to subunits which contain only one (alpha or beta) polypeptide occurs at 40 C (for Hb1) and at 50 C (for Hb2).

Alleles↗
PubMed1984

A proton nuclear magnetic resonance investigation of human hemoglobin A2. Implications on the intermolecular contacts in sickle hemoglobin fibers and on the Bohr effect of human normal adult hemoglobin.

High-resolution proton nuclear magnetic resonance spectroscopy at 300 and 600 MHz has been used to investigate the conformation of a minor hemoglobin component of human blood, hemoglobin A2 (alpha 2 delta 2), in solution. We have found that (i) the replacement of the beta chains by the delta chains in hemoglobin A2 conserves the alpha 1 delta 2 interface but slightly perturbs the alpha 1 delta 1 interface, and (ii) one surface histidine residue in the deoxy form and one in the carbonmonoxy form of hemoglobin A2 have local conformations and/or electrostatic environments which are different from the corresponding ones in human normal adult hemoglobin. By comparing the proton nuclear magnetic resonance titration of individual histidine residues in hemoglobin A2 and in human normal adult hemoglobin, we can conclude that in human normal adult hemoglobin, both beta 116 and beta 117 histidine residues are titratable in both the deoxy and the carbonmonoxy forms. Thus, these two histidine residues can contribute to the Bohr effect of human normal adult hemoglobin. The present nuclear magnetic resonance data on hemoglobin A2 and those previously obtained in our laboratory on sickle hemoglobin suggest that the antisickling property of hemoglobin A2 does not originate from an alteration of the intermolecular contact site at the beta 6 position, but involves additional amino-acid residues which are different in the beta and delta chains. We have found that the replacement of the beta 116 and beta 117 histidine residues in the delta chains does not play a significant role in the antisickling effect of hemoglobin A2 and, thus, these amino-acid residues do not participate in the intermolecular interactions responsible for the polymerization of sickle hemoglobin.

Carboxyhemoglobin↗
PubMed1979

Low proportions of glycosylated hemoglobin associated with hemoglobin S and hemoglobin C.

Using a cation-exchange chromatographic method, we found normal or subnormal values for glycosylated hemoglobin in a few diabetic patients with persistent hyperglycemia. Subsequent investigations revealed that these unexpected results had originated from black patients with diabetes. In view of common occurrence of abnormal hemoglobins in the Negro population, we subjected blood preparations to electrophoresis on cellulose acetate and acrylamide gel. The results have shown the presence of hemoglobin S or hemoglobin C in each patient. When allowance was made for the percentage of the abnormal hemoglobin, the "corrected values" of glycosylated hemoglobin increased to the diabetic range. Furthermore, the corrected values agreed well with the "expected values" calculated from a regression line correlating fasting blood glucose concentrations and proportions of glycosylated hemoglobin in more than 300 diabetics with no evidence of hemoglobinopathy. We conclude that in diabetic patients presenting with hemoglobin S or hemoglobin C, there is a considerable decrease in the values for glycosylated hemoglobin as measured by cation-exchange chromatographic methods, and that this decrease is proportional to the percentage of the abnormal hemoglobin.

Blood Glucose↗
PubMed1983

Interference of fetal hemoglobin and labile glycosylated hemoglobin with measurements of glycosylated hemoglobin.

We examined the effect of fetal hemoglobin and labile glycosylated hemoglobin on a number of diverse methods used to measure glycosylated hemoglobin. Samples were supplemented with various amounts of cord blood to give proportions of fetal hemoglobin ranging from 1 to 20% of total hemoglobin concentration. Procedures in which the separation of hemoglobin A1 from the major hemoglobin A fraction is based on differences in ionic properties (cation-exchange chromatography and electrophoresis) are subject to interference by fetal hemoglobin, whereas procedures that base the quantitation on other properties (colorimetry and affinity column chromatography) are not. The same procedures that are affected by the presence of fetal hemoglobin are also subject to interference by labile glycosylated hemoglobin. We conclude that the affinity chromatographic and colorimetric methods may give a more nearly accurate determination of glycosylated hemoglobin.

Chromatography, Affinity↗
PubMed1976

Hemoglobin pyrgos alpha2 beta2 83 (EF7) Gly leads to Asp: a new hemoglobin variant in double heterozygosity with hemoglobin S.

An electrophoretically fast-moving hemoglobin variant was found to be present together with hemoglobin S, in the hemolysate of the rythrocytes of at 3-yr-old Greek boy. Electrophoresis of the parents' erythrocyte hemolysates revealed that the father was an AS heterozygote, while the mother was a carrier of the variant hemoglobin. A sibling was also found to be a carrier. The amount of the mutant hemoglobin in the peripheral blood of the propositus, his mother, and his brother was 62.2%, 52.5%, and 51.1%, respectively, as determined by column chromatography. The patients peripheral blood smear showed mild anisocytosis, microcytosis, and hypochromia. Similar but less pronounced red cell abnormalities were found in the other two carriers. Structural analysis of the variant hemoglobin revealed substitution of an aspartic acid for the glycine residue at the beta83 (EF7) position. This new hemoglobin was named hemoglobin Pyrgos. All the carriers of hemoglobin Pyrgos are clinically healthy, and there seems to be no interaction between hemoglobin Pyrgos and hemoglobin S as manifested clinically.

Amino Acids↗
PubMed1970

The role of hemoglobin heme loss in Heinz body formation: studies with a partially heme-deficient hemoglobin and with genetically unstable hemoglobins.

A number of mutant hemoglobins are inordinately unstable, denaturing in circulating red cells into Heinz bodies, resulting in congenital Heinz body hemolytic anemia (CHBHA). We have emphasized that most such hemoglobins involve amino acid substitutions at sites neighboring the heme group of the beta-polypeptide chain, and have shown that heme binding to globin is diminished thereby. Thus, hemes were progressively lost from four unstable hemoglobins (Köln, Hammersmith, San Francisco, and Zürich) as they precipitated into Heinz bodies at 50 degrees C. The role of heme loss, especially from beta chains, in Heinz body formation was supported by studies with a hemoglobin synthesized to contain hemes only on its alpha chains (alpha(2) (heme)beta(2) (0)). The behavior of this compound, postulated to be an intermediary in the formation of Heinz bodies, mimicked that of the genetically unstable hemoglobins in several ways: (a) it precipitated at 50 degrees C into typical coccoid Heinz bodies; (b) as also observed with CHBHA hemoglobins this denaturation was virtually prevented by the heme ligands, cyanide or carbon monoxide, which inhibit further heme loss; it was potentiated by oxidation of hemes to the ferri- state, which accentuates heme loss; (c) the thiol groups of alpha(2) (heme)beta(2) (0) were hyperreactive, forming mixed disulfides with glutathione and membrane sulfhydryls at rates similar to those of CHBHA hemoglobins and 10 or more times that of normal hemoglobin A; (d) heme repletion of the protein molecules by the addition of crystalline hemin to either alpha(2) (heme)beta(2) (0) or to the genetically unstable hemoglobins, prevented their precipitation into Heinz bodies and normalized their aberrant electrophoretic behaviors; and (e) during Heinz body formation at 50 degrees C both alpha(2) (heme)beta(2) (0) and the genetically unstable hemoglobins released free alpha(heme)-chains into solution, suggesting that the bulk of the whitish, Heinz body precipitate is naked beta(8)-chains. We conclude that heme loss from mutant beta chains is an early step in Heinz body formation in several of the unstable hemoglobinopathies. The resulting hemedepleted compounds, of which synthetic alpha(2) (heme)beta(2) (0) is a prototype, are unstable, cleaving into beta(0)-chain precipitates (the bulk of the Heinz body material) and soluble, free alpha(heme)-chains (demonstrated previously in hemolysates from many patients with CHBHA).

Anemia, Hemolytic, Congenital↗
PubMed2001

Atypical hemoglobin H disease in a Thai patient resulting from a combination of alpha-thalassemia 1 and hemoglobin Constant Spring with hemoglobin J Bangkok heterozygosity.

A case of hemoglobin H disease in combination with hemoglobin Constant Spring and a beta-globin chain variant is reported in a 3-yr-old Thai girl. On routine cellulose acetate electrophoresis, one abnormal band in addition to the hemoglobins A, A2, H, Bart's and Constant Spring was detected. The amount of this abnormal band movement towards more anodic to the hemoglobin A was 35.7%. DNA analysis of the alpha-globin gene cluster by polymerase chain reaction (PCR) revealed a combination of defects caused by the SEA-type alpha-thalassemia 1 and the alpha-Constant Spring gene. Analysis of beta-globin gene by PCR and DNA sequencing also detected the heterozygosity for the GGC-GAC mutation at codon 56, leading to a substitution of aspartic acid for glycine resulting in the hemoglobin J Bangkok. The hematologic data of this unusual case of hemoglobin H disease are presented and compared with two compound heterozygotes for hemoglobin J Bangkok and alpha-thalassemia 1 found in the patient's father and grandfather. A simple DNA assay based on an allele-specific PCR for rapid diagnosis of the hemoglobin J Bangkok is also described.

Child, Preschool↗
PubMed1992

Differentiation of homozygous hemoglobin E from compound heterozygous hemoglobin E-beta O-thalassemia by hemoglobin E mutation analysis.

OBJECTIVES: To facilitate the differential diagnosis of hemoglobin FE in newborn infants (homozygous hemoglobin E vs hemoglobin E-beta O-thalassemia). METHODS: The beta-globin gene in DNA from infants found to have hemoglobin FE in the California newborn screening program was amplified by the polymerase chain reaction, and the product was digested with Mnl I, which fails to cut the product when the hemoglobin E mutation is present. When both amplified alleles fail to be cut, homozygous EE is diagnosed. If only one allele is cut, a beta-globin allele without the E mutation is present (non-E), which is most likely a gene with a beta O-thalassemia mutation. RESULTS: Samples from 18 infants revealed an EE genotype, and from two samples a non-E/E genotype was determined. Clinical examination of these two patients confirmed a diagnosis of hemoglobin E-beta O-thalassemia. An independent clinical diagnosis agreed with DNA analysis for all 17 of the 20 infants for whom follow-up and family studies were available. The DNA results were obtained within a week, but the clinical diagnoses often could not be resolved unequivocally for months. CONCLUSIONS: The direct analysis of patient DNA samples for the hemoglobin E mutation allowed rapid and accurate diagnosis in this sample of infants with hemoglobin FE on the newborn screen. This rapid discriminatory test should reduce cost and simplify the diagnostic approach for these patients, which currently consists of expensive and lengthy follow-up until clinical data and family studies result in a diagnosis.

Asian↗