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PubMed2004

A natural compound (reuterin) produced by Lactobacillus reuteri for hemoglobin polymerization as a blood substitute.

Stroma-free hemoglobin (Hb) has been modified by pyridoxylation and followed by polymerization with glutaraldehyde as a blood substitute. Nevertheless, the reaction rate of pyridoxylated Hb (PLP-Hb) with glutaraldehyde is too fast to control its molecular weight distribution. Additionally, it was reported that glutaraldehyde is cytotoxic even at low doses. To overcome these problems, another aldehyde, beta-hydroxypropionaldehyde (beta-HPA), was used in the study to polymerize hemoglobin (PLP-Hb). beta-HPA is a natural compound (reuterin) produced by Lactobacillus reuteri. It was found that the maximum degree of PLP-Hb polymerization by reuterin (RR-PLP-Hb) was approximately 40% if the formation of high molecular (> 500 kDa) polymers should be prevented. In contrast, at the same reaction condition, the glutaraldehyde-polymerized PLP-Hb solution became gel-like, due to overpolymerization. This indicated that the rate of PLP-Hb polymerization by reuterin was significantly slower than that by glutaraldehyde. With increasing the reaction temperature, PLP-Hb concentration, or reuterin-to-PLP-Hb molar ratio, the time to reach the maximum degree of PLP-Hb polymerization by reuterin became significantly shorter. Removal of unpolymerized PLP-Hb from the RR-PLP-Hb solution can be effectively achieved by a gel-filtration column. The P(50) value of the unmodified Hb solution was 14 torr, while that of the RR-PLP-Hb solution was 20 torr, an indication of lower oxygen affinity. Additionally, the oxygen-Hb dissociation curves for both test solutions had a sigmodial shape and a nearly 100% saturation at 100 torr. In the in vivo study, it was found that the animals treated with the RR-PLP-Hb solution all survived and remained healthy more than 3 months. In contrast, only one out of six rats survived for the control group treated with the unmodified Hb solution. Furthermore, it was found that the RR-PLP-Hb solution resulted in a significantly longer circulation time ( approximately 12 h) than the unmodified Hb solution ( approximately 1.5 h). These results suggest that the reuterin-polymerized PLP-Hb solution may be a new option in the development of blood substitutes.

Aldehydes↗
PubMed1973

Pyridoxal compounds as specific reagents for the alpha and beta N-termini of hemoglobin.

Bifunctional pyridoxal derivatives with a charged side chain in the 5' position react specifically with the N-terminal valine residues of hemoglobin. Three of these compounds, which have only a single negative charge in the side chain, are highly selective for the alpha-chain N-terminal residues in the oxy conformation while pyridoxal phosphate, with two negative charges, reacts specifically with the beta N-terminal in deoxyhemoglobin. Schiff's base formation, therefore, results in decreased oxygen affinity with pyridoxal phosphate but increased oxygen affinity with the other three compounds. Reduction with sodium borohydride leads to irreversible coupling at either end of the molecule, and preparation and properties of such derivatives are described.

Binding Sites↗
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↗
PubMed2002

Evidence for nonhydrogen bonded compound II in cyclic reaction of hemoglobin I from Lucina pectinata with hydrogen peroxide.

Studies that elucidate the behavior of the hemoglobins (Hbs) and myoglobins upon reaction with hydrogen peroxide are essential to the development of oxygen carrier substitutes. Stopped-flow kinetics and resonance Raman data show that the reaction between hydrogen peroxide and oxygenated and deoxygenated ferric Hb I (oxy- and deoxy-HbI) from Lucina pectinata produce compound I and compound II ferryl species. The rate constants ratio (k23/k41) between the formation of compound II from compound I (k23) and the oxidation of the ferrous HbI (k41, i.e., 25 M(-1) s(-1)) of 12 x 10(-4) M suggests that HbI has a peroxidative capacity for removing H2O2 from solution. Resonance Raman presents the formation of both, met-aquo-HbI and compound II ferryl species in the cyclic reaction of HbI with H2O2. The ferric HbI species is maintained by the presence of H2O2; it can produce HbI compound I, or it can be reduced to a deoxy-HbI derivative to form HbI compound II upon reaction with H2O2. The compound II ferryl vibration frequency appears at 805 and 769 cm(-1) for HbIFe(IV)=(16)O and HbIFe(IV)=(18)O species, respectively. This ferryl mode indicates the absence of hydrogen bonding between the carbonyl group of the distal Q64 and the HbIFe(IV)=O ferryl moiety. The observation suggests that both the trans-ligand effect and the polarizabilty of the HbI heme pocket are responsible for the observed ferryl oxo vibrational energy. The vibrational mode also suggests that the carbonyl group of the distal Q64 is oriented toward the iron of the heme group, increasing the distal pocket electron density.

Animals↗
PubMed2002

Development of a flow-injection analysis (FIA) enzyme sensor for fructosyl amine monitoring.

An enzyme-sensor system with flow-injection analysis (FIA) has been developed for the detection of fructosyl amine compounds; the sensor utilizes fructosyl amine oxidase isolated from the marine yeast Pichia sp. N1-1 strain. With this FIA system 0.2 to 10 mmol L(-1) fructosyl valine can be determined. The sensor is approximately five times more sensitive to fructosyl valine, a model compound for glycated hemoglobin HbA1c, than to N(epsilon)-fructosyl lysine, a model compound for glycated albumin. This FIA system can also be used to detect fructosyl dipeptides. The operational stability of the sensor enabled more than 120 consecutive sample injections over a period of approximately 20 h.

Amino Acid Oxidoreductases↗
PubMed2004

Molecular and hematological characterization of hemoglobin Hope/hemoglobin E and hemoglobin Hope/alpha-thalassemia 2 in Thai patients.

We report the hematological and molecular characterization of compound heterozygosity for hemoglobin (Hb) Hope/Hb E and double heterozygosity for Hb Hope/ alpha-thalassemia 2 found in 2 unrelated Thai individuals. The first proband presented with slight anemia and mild hypochromic microcytosis. Routine cellulose acetate Hb electrophoresis at pH 8.6 revealed in addition to Hb E another variant migrating slightly more anodic to Hb A. On cation exchange high-pressure liquid chromatography, the variant was eluted in the amount of 60.9% after Hb E The same abnormal Hb was found in a second family in which the proband and her younger sister were both double heterozygotes for this Hb variant and deletional alpha-thalassemia 2, whereas an older sister was a pure carrier of the variant. The amounts of this variant were found to be 34.9%, 35.4%, and 38.3% in the proband, her younger sister, and her older sister, respectively. Direct DNA sequencing of the amplified beta-globin genes of both probands identified the GGT (Gly)-GAT (Asp) mutation at codon 136 corresponding to Hb Hope. beta-Globin gene haplotype analysis demonstrated that all the Thai betaHope genes were associated with the same haplotype, (+ - - - - + +), indicating a single origin of this variant in Thailand. A simple method based on allele-specific polymerase chain reaction for accurate diagnosis of the Hb Hope is described.

Adult↗
PubMed1979

Multiple hemoglobins in Triturus cristatus: their degradation by sulfhydryl compounds.

1. Hemolysates of newt (Triturus cristatus) red cells contain four distinct hemoglobin species which have been observed consistently both in individual animals and pooled samples. 2. Hemoglobin heterogeneity in the species arises from existence of multiple hemoglobulins, with no indication of genetic polymorphism. 3. While the relative proportions of the different hemoglobins may vary in different samples, HbII is usually the most abundant, with HbIII and HbIV constituting most of the remainder of the total hemoglobin complement. HbI never exceeds 3-5% of the total hemoglobin. 4. Neither the electrophoretic migration nor the anion exchange properties of the four hemoglobin species are altered by conversion of oxyhemoglobin to the cyanmet derivative, excluding artifacts due to different oxidation states of iron. 5. The average molecular weight of newt total hemoglobulin is 67,182 with no indication of hemoglobin polymers. 6. The use of sulfhydryl-reducing agents (mercaptoethanol, dithiothreitol) as a precaution against aggregation results in extensive degradation of newt hemoglobin through a process similar to "coupled oxidation" by ascorbate. 7. The degradative effects of sulfhydryl-reducing agents on newt hemoglobin suggest that these reagents be used cautiously in any hemoglobin analysis.

Animals↗
PubMed1976

The fate of phenylhydroxylamine in human red cells.

Phenylhydroxylamine added to human red cells under aerobic conditions and in the presence of glucose was partly reduced to aniline. About half the hydroxylamine was recovered as amine after a 2-hr incubation. The aniline, after acetylation, was identified as acetanilide by melting point, Rf-value in TCL as well as UV, IR, and NMR spectroscopy. The fate of the remaining phenylhydroxylamine was followed by use of 14C-labeled phenylhydroxylamine. About 30% of the total radioactivity was bound to hemoglobin or other proteins and about 20% was found in highly polar low-molecular substances which were insoluble in organic solvents. The elucidation of the sites at which phenylhydroxylamine was bound to hemoglobin was complicated by the lability of the bonds. When purified human hemoglobin had reacted with radioactive phenylhydroxylamine, large proportions of the radioactivity bound to hemoglobin were removed by treatment with acid or with PMB for separation of alpha- and beta-chains. The radioactive compound liberated from hemoglobin by acid was found to be aniline. After reaction with phenylhydroxylamine the number of SH groups titrable with PMB was found to be diminished. Pretreatment of hemoglobin with N-ethylmaleimide or PMB decreased the amount of phenylhydroxylamine bound to hemoglobin but did not fully prevent the reaction. Tryptic digestion of hemoglobin after reaction with radioactive phenylhydroxylamine yielded tryptic peptides with lower specific activity than that of hemoglobin. Chymotryptic digestion of the tryptic core yielded a core with specific activity much higher than that of hemoglobin. Fingerprinting of the tryptic or chymotryptic hydrolyzates showed the presence of peptides with high and other ones with low or no radioactivity and of radioactive compounds which did not react with ninhydrin. In the covalent binding of phenylhydroxylamine to globin the SH group beta93 plays an important role, but other yet unknown sites are also reactive.

Acetanilides↗
PubMed1978

Inhibition of sickle hemoglobin gelation by amino acids and related compounds.

The effects of amino acids, several aromatic compounds, and peptides on the gelation and solubility of deoxyhemoglobin S have been studied. The aromatic amino acids (tryptophan, phenylalanine, and possibly tyrosine) significantly inhibited the rate of gel formation and increased solubility. The dipeptide L-Thr-L-Phe, the tripeptide L-Lys-L-Phe-L-Phe, and various phenylalanine analogues (hydrocinnamic acid, phenethylamine, benzamine, and amphetamine) also inhibited gelation. However, aromaticity is not a sufficient condition for inhibiting gelation as shown by the fact that several aromatic compounds (acetylsalicylic acid, salicyclic acid, aniline, and phenol) enhanced gelation. Surprisingly, several oligopeptides (betaS1--12, betaS4--8, betaS3--13, and betaS4--10) also enhanced gelation. All of these additives follow the supersaturation relationship that the delay time for gelation is proportional to the ratio of the total hemoglobin concentration to the solubility of deoxyhemoglobin S to the nth power (n approximately 35). A possible mechanism for the action of these inhibitors is considered in terms of a specific site of interaction on the hemoglobin molecule. Although none of these compounds may prove to be efficacious in treatment of sickle cell anemia, they should yield information about the structure and process of formation of the deoxyhemoglobin S gel.

Amino Acids↗
PubMed1979

Intracranial vasospasm: a study with iron compounds.

The effects of topically applied hemoglobin, methemoglobin, hemin, ferrous chloride (FeCl2) and ferric chloride (FeCl3) were investigated by observation through the operating microscope to determine their effect on the normal and spastic canine basilar artery. Following transclival exposure, the artery was made spastic by puncture or topical barium chloride. No consistent changes in arterial diameter were seen with topical hemoglobin, methemoglobin, or hemin. The buffered ferrous ion (Fe++) caused marked vasodilation at concentrations of 10 microgram/ml. The buffered ferric ion (Fe++) caused mild vasoconstriction at similar concentrations. The possible role of iron (a component of hemoglobin) in vasospasm following subarachnoid hemorrhage and subsequent hemoglobin degradation is discussed.

Animals↗
PubMed1984

Hemoglobin. A biologic fenton reagent.

Iron and iron compounds may facilitate hydroxyl-radical generation from activated oxygen species. Earlier work on the generation of this radical has been focused on simple, low-molecular-weight iron compounds. We hypothesized that free hemoglobin, like other iron-rich substances, might also mediate hydroxyl-radical generation. We find: 1) In the presence of a superoxide anion-generating system (hypoxanthine and xanthine oxidase), hemoglobin promotes hydroxyl-radical formation in a dose-dependent fashion. 2) This generation of hydroxyl radical is greatly decreased by prior oxidation of the hemoglobin, equilibration of hemoglobin with carbon monoxide, or addition of catalase, while added superoxide dismutase has little effect. Therefore, hydroxyl radical probably arises primarily via reaction between the ferrous heme iron and H2O2. 3) In further support of this, hydroxyl radical forms as readily upon the addition of H2O2 to hemoglobin. 4) Hemoglobin also increases hypoxanthine/xanthine oxidase-driven peroxidation of poly-unsaturated fatty acids such as arachidonic acid and human red cell membrane lipids. 5) The addition of sufficient haptoglobin (the plasma hemoglobin-binding protein) suppresses both hemoglobin-driven hydroxyl radical and malondialdehyde generation. Thus, free hemoglobin may be biologically hazardous, in part because it acts as a "Fenton" reagent, having the potential to catalyze hydroxyl-radical generation in areas of inflammation. Haptoglobin, which binds hemoglobin very tightly, blocks this through a presently unknown mechanism. An important physiologic function of haptoglobin may be prevention of such hemoglobin-mediated oxidation.

Arachidonic Acid↗
PubMed1978

Model compounds for the T state of hemoglobin.

O2 binding to a series of ferrous and cobaltous "picket fence" porphyrins is reported. N-Methylimidazole and covalently attached imidazoles gives O2 binding to ferrous porphyrins with deltaH degrees =-16.2 kcal/mol (-67.7 kJ/mol) and deltaS degrees =-40 eu (standard state, 1 atmosphere O2). Similar studies with cobaltous porphyrins yield deltaH degrees =- 12.8 kcal/mol (-53.5 kJ/mol) and deltaS degrees =- 39 eu. These values match well those of myoglobin and isolated subunits of hemoglobin and their cobalt reconstituted analogues. 1,2-Dimethylimidazole has been successfully used to mimic the presumed restraint of T state hemoglobin. In direct analogy to the decreased cooperativity shown by cobalt-substituted hemoglobin, model cobalt porphyrins show a smaller decrease in O2 affinity than the analogous iron porphyrins when the axial base is hindered. Thermodynamic data are presented. The molecular mechanism of cooperativity in hemoglobin is discussed.

Cobalt↗