Fetal hemoglobin variants in mice

Two strains of mice, DBA and C3H, have a fetal globin polypeptide chain which differs in electrophoretic mobility from the corresponding fetal chain of the C57B1 strain. Mice of the DBA and C3H strains also differ from those of the C57B1 in adult hemoglobin type. Results of backcrossing the (DBA x C57B1) hybrid to the C57B1 suggest that the fetal chain locus and the adult beta-chain locus are closely linked.     

Hemoglobin Portland 1: a new human hemoglobin unique in structure

A new hemoglobin (Hb), Portland 1, has been found in a newborn infant having multiple congenital anomalies and complex autosomal chromosomal mosaicism. The new hemoglobin has a unique tetrameric structure (molecular weight, 66,000) composed of two pairs of different types of chains, neither of which is alpha, gamma(2)x(2). The x-chain of Hb Portland 1 may be a new type of hemoglobin chain, but the available evidence suggests that it may be identical with the epsilon chain. We suggest that Hb Portland 1 is an embryonic hemoglobin that persisted until after birth in relatively large amounts in this patient.     

Hemoglobin Hijiyama: a new fast-moving hemoglobin in a Japanese family

A variant of hemoglobin A, named Hb Hijiyama, found in two generations of a Japanese family living in Hiroshima, Japan, has a higher anodal electrophoretic mobility than hemoglobin A; a gain of two negative charges per molecule is indicated. Fingerprinting and amino acid analysis showed the biochemical anomaly to be in the beta chain at residue 120, where lysine is replaced by glutamic acid. In the heterozygote carriers of the abnormal hemoglobin there is no apparent association with clinical or hematologic abnormalities.     

Hemoglobin Sphakiá: a delta-chain variant of hemoglobin A2 from Crete

A new variant of the normal minor component Hb A(2) has been detected in a family that lives in Sphakiá, Crete. Chemical studies of this abnormal hemoglobin, designated Hb A(2) delta Sphakiá, indicates a substitution of the histidyl residue number two of the delta-chain by an arginyl residue.     

Hemoglobin Freiburg: abnormal hemoglobin due to deletion of a single amino acid residue

Structural characterization of a new variant of human hemoglobin (adult), designated hemoglobin Freiburg, indicates the deletion of the valyl residue No. 23 from an otherwise normal beta-chain. The formula may be written (alpha2)beta(2)(23val-0). The abnormal hemoglobin is present with hemoglobin A in the proposita and in two of her three living children, but is not detectable in her parents. We postulate that this variant represents a triplet base deletion which most likely resulted from an unequal crossing-over between two normal betachain loci during meiosis in one of the parents of the proposita.     

Hemoglobin J-Korat in Thais

Hemoglobin J(Korat), a "fast" hemoglobin with an anomaly in its beta chain different from the anomalies previously reported, was the major hemoglobin component in the blood of nine subjects among 1923 Thais from northeastern Thailand. After hemoglobin E, J(Korat) is the second most frequent of the anomalous hemoglobins among Thais.     

Hemoglobin: molecular changes during anuran metamorphosis

Anuran metamorphosis is accompanied by changes in the sedimentation patterns of the lysates of red blood cells of several species. Rana grylio and Rana catesbeiana tadpoles have hemoglobins that sediment at 4.3S (molecular weight, 68,000) and gradually produce a heavier 7.0S component (estimated molecular weight, 136,000) during metamorphosis to the adult frog. There is extensive change in the amino acid compositions of these hemoglobins; these changes may account for observed changes in electrophoretic mobility.     

Gelation of sickle cell hemoglobin: effects of hybrid tetramer formation in hemoglobin mixtures

The altered gelation behavior found in mixtures of sickle cell hemoglobin with other hemoglobins is due to the formation of hybrid hemoglobin tetramers from unlike dimers. The hemoglobins need not possess the deoxy quaternary structure for gelation to occur; liganded forms are also capable of participation in gelation.     

Hemoglobin polymorphism in Macaca nemestrina

Four hemoglobin phenotypes have been noted in the pigtailed monkey ( Macaca nemestrina). Pedigree studies suggest a simple codominant Mendelian explanation for inheritance of three of these phenotypes, including one electrophoretically identical with human type A. The fourth type occurred in only one animal in this series.     

Hemoglobin Rainier (beta145 Tyrosine rarr Histidine): Alkali-Resistant Hemoglobin with Increased Oxygen Affinity

Hemoglobin Rainier, a new hemoglobin variant associated with erythrocytosis, was found in six members of a Caucasiant family. Structurally, it represents substitution of histidine for the invariant residute H23 tyrosine in the beta-hemoglobin polypeptide chain (beta(145) tyrosine --> histidine). Hemoglobin Rainier is the first example of a single amino acid substitution in adult human hemoglobin, causing increased resistance to alkali denaturation.     

Hemoglobin patterns in American Indians

Two populations of North Carolina have been analyzed for hemoglobin patterns by paper electrophoresis. Of 534 Cherokee Indians, both mixed and full bloods, all showed normal hemoglobin. Lumbee Indians of less certain ethnic status had 1.7 percent of hemoglobin S, an equal amount of hemoglobin C, and one possible hemoglobin D trait among 1332 bloods studied.     

Rabbit hemoglobin biosynthesis: use of human hemoglobin chains to study molecule completion

A cell-free protein-synthesizing system made from rabbit reticulocytes was used to incorporate (14)C-amino acids into hemoglobin. Electrophoretic analyses of the soluble products of this cell-free system revealed a fraction containing rabbit (14)C-alpha chains in addition to the rabbit (14)C-hemoglobin. The addition of isolated human hemoglobin beta chains to this system during active synthesis inhibited the release of newly synthesized rabbit (14)C-beta chains into solution from the ribosome fraction. This inhibition was possibly a result of hybrid hemoglobin formation between rabbit alpha and human beta chains. A model of hemoglobin construction in which soluble alpha chains are intermediates is suggested. These alpha chains may aid in the release of beta chains from the polyribosomes during the completion of the hemoglobin molecule.     

Hemoglobin Lepore trait: globin synthesis in bone marrow and peripheral blood

There was decreased synthesis of the beta-globin chain in the peripheral blood, and equal synthesis of alpha- and non-alpha-chains in the bone marrow of three patients with hemoglobin Lepore trait, similar to the findings in patients with heterozygous beta-thalassemia. There is a relative instability of the synthetic mechanism for normal beta-chain in these patients.     

超滤在猪血红蛋白酶解液中的应用研究

采用6～10 kD和3 kD超滤膜对猪血红蛋白水解液进行浓缩实验,对超滤前后的多肽类蛋白质、氨基氮、血红素的变化进行分析.实验结果表明:采用3 kD超滤膜对酶解液的浓缩效果较好,浓缩倍数分别达到2.3、2.0、1.9,经冷冻干燥得产物蛋白质多肽含量91%,血红素含量2.9%混合营养物,可以用来制备含量较高的富含血红素肽的混合营养物.     

Hemoglobin interaction: modification of solid phase composition in the sickling phenomenon

Direct analyses of solid phase formed by deoxygenating solutions of sickle-cell hemoglobin (Hb S) in the presence of certain other hemoglobin species show that hemoglobins A and C can participate in the filamentous fine structure characteristic of the sickling phenomenon. In contrast, fetal hemoglobin (Hb F) is nearly completely excluded.     

Conformational equilibria in spin-labeled hemoglobin

A component characteristic of deoxyhemoglobin appears in the paramagnetic resonance spectrum of spin-labeled oxyhemoglobin, and vice versa, under conditions of pH and ionic strength consistent with the interpretation that the spectrum is sensitive to the conformational equilibrium of the carboxy-terminal histidines. The oxygenation-induced change in the resonance spectrum is discussed in terms of shifts in this equilibrium.     

Hemoglobin as a tracer in hemodynamic pulmonary edema

Stroma-free hemoglobin is an electron-opaque molecule useful as a tracer for the ultrastructural stuty of pulmonary capillary permeability. After this tracer was infused into the isolated pulmonary lobe of the dog, the endothelial junctions of the capillaries, as revealed by electron microscopy, act like distensible pores, thus allowing the tracer to escape when the pulmonary artery pressure was raised above 50 millimeters of mercury.