Sea cucumber sibling species: polypeptide chain types and oxygen equilibrium of hemoglobin

The hemoglobin of the "thin" sibling species of Thyonella gemmata (phylum: Echinodermata; class: Holothuria) has three electrophoretically distinct polypeptide chains. In "stout" sibling species of T. gemmata there are only two chain types. These results account for the greater number of multiple hemoglobins in "thins" than in "stouts," as well as for differences in the amounts of some of the multiple hemoglobins when comparisons are mnade of hemolyzates of erythrocytes from the water vascular systemn and from the main body cavity of the "thin" but not the "stout" sibling species.     

Evolution of oxygen secretion in fishes and the emergence of a complex physiological system

We have reconstructed the events that led to the evolution of a key physiological innovation underpinning the large adaptive radiation of fishes, namely their unique ability to secrete molecular oxygen (O2). We show that O2 secretion into the swimbladder evolved some 100 million years after another O2-secreting system in the eye. We unravel the likely sequence in which the functional components of both systems evolved. These components include ocular and swimbladder countercurrent exchangers, the Bohr and Root effects, the buffering power and surface histidine content of hemoglobins, and red blood cell Na+/H+ exchange activity. Our synthesis reveals the dynamics of gains and losses of these multiple traits over time, accounting for part of the huge diversity of form and function in living fishes.     

Oxygen equilibrium of brachiopod Lingula hemerythrin

In contrast to hemerythrin from five different species of sipunculid worms, ecardine brachiopod Lingula hemerythrin has an oxygen equilibrium which is reversibly altered by pH changes, both the oxygen affinity (Bohr effect) and the interactions between oxygen-binding centers being a function of pH. The significance of these phenomena is discussed in view of the phylogenetic distribution of hemerythrin and the function of respiratory pigments.     

Bohr Effect: Absence in a Molluscan Hemocyanin

The hemocyanin of the keyhole limpet, Diodora aspera, shows no Bohr effect within the pH range 6.88 to 7.84. At 10 degrees C the pressure of half-saturation is 5 mm-Hg of oxygen pressure. A moderately positive interaction occurs among the oxygen-combining sites during oxygenation. The heat of oxygenation is calculated to be approximately -12.6 kcal/mole of oxygen. The pH of normal blood of Diodora is lower than that of many other marine molluscs.     

Oxygenation properties of snake hemoglobin

Natrix taxispilota hemoglobin has a very high oxygen affinity which depends upon pH in an unusual manner. The oxygen affinity increases slightly upon protein dilution, but the pK's of the Bohr groups are unchanged. Oxidation promotes hemoglobin polymerization, which can be inhibited by prior treatment with iodoacetamide. Reaction with iodoacetamide also causes a slight increase in the oxygen affinity, no change in the pK's of the Bohr groups, and a drastic reduction in heme-heme interaction.     

Cat hemoglobin: pH-dependent cooperativity of oxygen binding

Cat hemoglobin has a lower cooperativity and oxygen affinity than most mammalian hemoglobins. In contrast to the usual invariance of cooperativity with pH, a rise in cooperativity with pH is predicted by the allosteric model for low-affinity hemoglobins. Such a pH-dependent cooperativity for cat hemoglobin has been found.     

Silent hemoglobin alpha genes in apes: potential source of thalassemia

Small quantities of unusual hemoglobins were found in 1 of 37 chimpanzees and 2 of 6 gorillas. In each genus these hemoglobins contain unique alpha chains that differ from the ordinary by eight to nine scattered amino acid changes. The unusual chains arise from a hitherto undetected hemoglobin (3)alpha locus. No (3)alpha products are found in most apes; accordingly, (3)alpha is considered synthetically inactive in all but a few reversion mutants. Indirect evidence that the inactive (3)alpha locus is juxtaposed to an active alpha locus together with the supposition that (3)alpha exists in man provides a setting wherein thalassemia might be produced by nonhomologous recombination between two loci.     

Oxygen binding in cyanmet hybrid and normal hemoglobins: applicability of sequential and two-state concerted models

The cyanmet hybrid hemoglobins alpha(2)beta(+CN)(2) and alpha(+CN)(2)beta(2) are widely held to be similar or equivalent in structure and subunit interactions to the partially oxygen-liganded species alpha(2)(beta * O(2))(2) and (alpha * O(2))(2)beta(2), respectively. An analysis of precise data on oxygen binding to the cyanmet hybrids and normal hemoglobin shows that if this is the case, then cooperative ligand binding in hemoglobin is more properly described by some model of the sequential type than by any twostate concerted model.     

Genetic Control of Hemerythrin Specificity in a Marine Worm

A biochemical polymorphism of coelomic hemerythrin has been found in the sipunculid Golfingia gouldii; the electrophoretically "fast" and "slow" coelomic hemerythrins differ in their oxygen equilibria and by a single peptide in tryptic and chymotryptic "fingerprints." All individuals of this sipunculid have the same vascular hemerythrin, which is electrophoretically different from any of the coelomic hemerythrins. Vascular and coelomic hemerythrins of another sipunculid, Dendrostomum cymodoceae, have quite different "fingerprints." Thus, on the basis of two separate types of evidence the tissue-specific hemerythrins appear to have a distinct genetic basis. The embryological and phylogenetic implications are discussed.     

Structural transitions upon ligand binding in a cooperative dimeric hemoglobin

Comparison of the 2.4 angstrom resolution crystal structures of dimeric clam hemoglobin in the deoxygenated and carbon-monoxide liganded states shows how radically different the structural basis for cooperative oxygen binding is from that operative in mammalian hemoglobins. Heme groups are in direct communication across a novel subunit interface formed by the E and F helices. The conformational changes at this interface that accompany ligand binding are more dramatic at a tertiary level but more subtle at a quaternary level than those in mammalian hemoglobins. These findings suggest a cooperative mechanism that links ligation at one subunit with potentiation of affinity at the second subunit.     

Oxygen affinity and electrolyte distribution of human blood: changes induced by propranolol

Propranolol causes a massive leakage of potassium ions from red cells, which results in an alteration of the Gibbs-Donnan equilibrium across the red cell membrane. According to such a mechanism, the presence of propranolol significantly increases the hydrogen ion activity of the interior of the red cell, causing a decreased oxygen affinity of hemoglobin according to the classical Bohr effect. No release of 2,3-diphosphoglycerate which may be bound to the membrane is thus necessary to explain the effect of propranolol on the oxygen dissociation curve of blood.     

Functional characteristics of the blood of the deep-sea hydrothermal vent brachyuran crab

Hemocyanin in the whole blood of the hydrothermal vent brachyuran crab, Bythograea thermydron, has a moderate oxygen affinity (P(50) = 6.6 millimeters of mercury at 2.6 degrees C; pH 7.5), which unlike that of other hemocyanins is independent of temperature over the range 2 degrees to 30 degrees C; carbon dioxide and pH have independent effects on the oxygen affinity of this pigment. The pH effect on affinity is moderate (Deltalog P(50)/DeltapH = -0.34), whereas increased carbon dioxide, which can act both directly and by changing pH, has a much larger effect (Deltalog P(50)/DeltapH = -0.81). This blood has a moderately high degree of cooperativity (Hill cooperativity coefficient, n, was 2.8) and a large oxygen-carrying capacity for a crustacean (4.5 milliliters of oxygen per 100 milliliters of blood). These properties characterize an oxygen transport system whose function appears to be largely independent of the wide range of environmental conditions encountered around the vents.     

灌漠土区吨粮田开发与持续农业建设

通过数值分析,认为灌淤土和灌漠土属同一土类,其中的微小差异应在亚类一级来区别。灌漠土占我国国土面积一半以上,在我国农业现代化建设中具有举足轻重的作用和战略地位。     

Multiplicity of hemoglobins in the genus Chironomus (Tendipes)

The number of hemoglobins found in individual mature larvae of several Chironomus species is six to nine. The consistency of this number and of the electrophoretic mobilities of these separable forms seems to indicate the synchronous production of polypeptide chains by several genetic loci.     

Localized control of ligand binding in hemoglobin: effect of tertiary structure on picosecond geminate recombination

The picosecond geminate rebinding of molecular oxygen was monitored in a variety of different human, reptilian, and fish hemoglobins. The fast (100 to 200 picoseconds) component of the rebinding is highly sensitive to protein structure. Both proximal and distal perturbations of the heme affect this rebinding process. The rebinding yield for the fast process correlates with the frequency of the stretching motion of the iron-proximal histidine mode (VFe-His) observed in the transient Raman spectra of photodissociated ligated hemoglobins. The high-affinity R-state species exhibit the highest values for VFe-His and the highest yields for fast rebinding, whereas low affinity R-state species and T-state species exhibit lower values of VFe-His and correspondingly reduced yields for this geminate process. These findings link protein control of ligand binding with events at the heme.     

Gene selection in hemoglobin and in antibody-synthesizing cells

Close linkage of mutually exclusive genes occurs in the non-alpha chain hemoglobin genes and in the immunoglobulin genes of man and other mammals. The expression of one gene in the cluster precludes the expression of any other linked gene. A simple, testable theory of gene selection called "looping-out excision"which was designed only to explain this mutual exclusivity in the hemoglobin system is described. The theory is closely concordant with a wide range of previously unexplained findings concerning hematopoiesis- including the developmental changes of hemoglobins, the increases in immature or fetal forms of hemoglobin that accompany anemia, and with the distribution of adult and fetal hemoglobins among erythrocytes during normal embryogenesis and in various pathological conditions. One corollary of this theory is that erythroid tissue in the normal adult bone marrow is constantly recapitulating the developmental stages of its embryogenesis. Another corollary is that the selection from among the linked globin genes occurs independently on the two chromosomes of the diploid organism. Both of these corollaries are supported by the available data. The same theory of gene selection is also remarkably consistent with known data for immunoglobulin synthesis; it could explain not only the mutually exclusive activation of linked variable genes but also the splicing which occurs between genetically linked variable and constant region genes for the immunoglobulin polypeptide chains. The agreement between these two different tissues is considered to be strong evidence that the proposed mechanism is correct at least in broad outline. Evidence from the genetics of maize and of drosophila also supports this theory of somatic tissue variegation. On the basis of these comparisons, I suggest that looping-out excision probably occurs also in other tissues and may be one means of gene selection and activation in differentiating cells.     

In situ formation of an oxygen-evolving catalyst in neutral water containing phosphate and Co2+

The utilization of solar energy on a large scale requires its storage. In natural photosynthesis, energy from sunlight is used to rearrange the bonds of water to oxygen and hydrogen equivalents. The realization of artificial systems that perform "water splitting" requires catalysts that produce oxygen from water without the need for excessive driving potentials. Here we report such a catalyst that forms upon the oxidative polarization of an inert indium tin oxide electrode in phosphate-buffered water containing cobalt (II) ions. A variety of analytical techniques indicates the presence of phosphate in an approximate 1:2 ratio with cobalt in this material. The pH dependence of the catalytic activity also implicates the hydrogen phosphate ion as the proton acceptor in the oxygen-producing reaction. This catalyst not only forms in situ from earth-abundant materials but also operates in neutral water under ambient conditions.     

Dynamics of elliptical galaxies

Elliptical galaxies were once thought to be similar in their structure and dynamics to rotationally flattened bodies like stars. The discovery that elliptical galaxies rotate much more slowly than a fluid body with the same shape has led to a qualitative change in our understanding of the dynamics of these systems. It is now believed that elliptical galaxies are fully triaxial in shape. Self-consistent triaxial equilibria have been constructed and appear to be long-lived; they are made possible by the existence of conserved quantities, or integrals of motion, for galactic potentials without rotational symmetry. Many self-consistent equilibria are unstable; the nonexistence of elliptical galaxies with axis ratios more extreme than 3:1 is probably the result of such an instability. There is evidence for strong central mass concentrations, perhaps massive black holes, at the centers of some nearby galaxies. Recent observations suggest that many elliptical galaxies formed through the merger of two or more spiral galaxies.     

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.     

Combined Effects of Excess Mn and Low pH on Oxidative Stress and Antioxidant Enzymes in Cucumber Roots

The effects of excess Mn on oxidative stress and antioxidant enzymes in cucumber roots under different pH （pH 4.5 and 6.5） were studied. The results indicated that lipid peroxidation was increasingly serious with the increased concentration of Mn, especially under low pH. As a result, the growth of cucumber roots and shoots was significantly inhibited. Excess Mn led to an elevation in activities of Mn-SOD and Fe-SOD, which played an important role in removing O2^-. CAT was sensitive to excess Mn, and its activity significantly decreased under excess Mn and low pH, while activities of GPX, APX, DHAR and GR increased under low pH and to some extent under excess Mn, which indicated their important roles in scavenging reactive oxygen in tolerance to low pH and excess Mn of cucumber roots.