The primary structure of three hemoglobin chains from the indigo snake (Drymarchon corais erebennus, Serpentes): First evidence for αD chains and two β chain types in snakes

The hemoglobin of the indigo snake (Drymarchon corais erebennus, Colubrinae) consists of two components, HbA and HbD, in the ratio of 1:1. They differ in both their alpha and beta chains. The amino acid sequences of both alpha chains (alpha(A) and alpha(D)) and one beta chain (betaI) were determined. The presence of an alpha(D)chain in a snake hemoglobin is described for the first time. A comparison of all snake beta chain sequences revealed the existence of two paralogous beta chain types in snakes as well, which are designated as betaI and betaII type. For the discussion of the physiological properties of Drymarchon hemoglobin, the sequences were compared with those of the human alpha and beta chains and those of the closely related water snake Liophis miliaris where functional data are available. Among the heme contacts, the substitution alpha(D)58(E7)His-->Gln is unusual but most likely without any effect. The residues responsible for the main part of the Bohr effect are the same as in mammalian hemoglobins. In each of the three globin chains only two residues at positions involved in the alpha1/beta2 interface contacts, most important for the stability and the properties of the hemoglobin molecule, are substituted with regard to human hemoglobin. On the contrary, nine, eleven, and six alpha1/beta1 contact residues are replaced in the alpha(A), alpha(D), betaI chains, respectively

Dimer-tetramer Transition In Hemoglobins From Liophis Miliaris-i. Effect Of Organic Polyphosphates

1. 1. Hemoglobin from the water-snake Liophis miliaris in the stripped form presents high oxygen affinity of about P50 = 1 mmHg and Hill coefficient of about 1.0 at pH from 6.8 to 8.5. 2. 2. In the presence of ATP such values become P50 = 20 mmHg and nH about 2.0, respectively, at low pH from 6.5 to 7.5. 3. 3. When the pH increases an abrupt decrease of both P50 and nH values occurs falling close to those found for the stripped hemoglobin. 4. 4. Gel-filtration in Sephadex G-100 equilibrated with 0.05 M Tris-HCl buffer containing 1 mM EDTA of the stripped hemoglobin show the presence of only one component of mol. wt of about 32,500 dt similar to the dimer of human hemoglobin A. 5. 5. The deoxy form of the dimer previously treated with ATP and placed on Sephadex column in the same condition but containing 1 mM IHP emerges as tetramer with mol. wt similar to that found for human hemoglobin, i.e. of about 65,000 dt. 6. 6. Results of the multiplicity of the snake hemoglobin, as well as the large alkaline Bohr effect in the presence of ATP previously reported, seems to be inconsistent due to the dimer-tetramer transition that occurs when ATP is bound to the stripped hemoglobin. 7. 7. A molecular mechanism involving the dimer-tetramer transition is proposed to described the oxygen transport in these animals. © 1987.864683687Atha, Riggs, Tetramer-dimer dissociation in hemoglobin and the Bohr effect (1976) J. biol. Chem., 251 (18), pp. 5537-5543Antonini, Brunori, The equilibrium of hemoglobin and myoglobin with ligands (1971) Hemoglobin and Myoglobin in Their Reaction with Ligands, pp. 153-186. , North Holland, AmsterdamChiancone, Gilbert, Dissociation of hemoglobin into subunits. I. Oxyhemoglobin: effect of acetic acid (1965) J. biol. Chem., 240, pp. 3866-3875Douglas, Haldane, Haldane, The laws of combination of haemoglobin with carbon monoxide and oxygen. (1912) J Physiol, 44, p. 275. , ApudSullivan, Riggs, The subunits dissociation properties of turtle hemoglobin (1967) Biochim. biophys. Acta, 140, pp. 274-283Focesi, Jr., Brunori, Bonaventura, Wilson, Galdames-Portus, Effect of pH on the kinetics of oxygen and carbon monoxide reactions with hemoglobins from the airbreathing fish, Loricarüchthys (1979) Comp. Biochem. Physiol., 62 A, pp. 169-171Heatwole, Seymour, Respiration of marine snakes (1976) Respiration of Amphibious Vertebrates, pp. 375-389. , G.M Hughes, Academic Press, LondonLaurent, Killander, A theory of gel filtration and its experimental verification (1964) Journal of Chromatography A, 14, pp. 317-325Matsuura, Ogo, Focesi, Jr., Multiplicity and immunological characterization of the haemoglobin components, from Liophis miliaris and Helicops modestus (1983) Comp. Biochem. Physiol., 76 B, pp. 915-919Monod, Wyman, Changeaux, On the nature of allosteric transitions: a pausible model (1965) J. molec. Biol., 12, pp. 88-118Ogo, Abe, Focesi, Jr., Oxygen dissociation constant in hemoglobin of Helicops modestus and Liophis miliaris, two water-snakes with different morphological adaptations to their environment (1979) Comp. Biochem. Physiol., 63 A, pp. 285-289Ogo, Matsuura, Focesi, Jr., Content of organic polyphosphates and their allosteric effects on haemoglobins from the water-snakes Helicops modestus and Liophis miliaris (1984) Comparative Biochemistry and Physiology Part A: Physiology, 18 A, pp. 587-589Rossi-Fanelli, Antonini, Studies on the oxygen and carbon-monoxide equilibria of human myoglobin (1958) Archives of Biochemistry and Biophysics, 77, pp. 428-492Sekino, Focesi, Bonaventura, Bonaventura, Functional properties of Aphysia brasiliana myoglobin (1978) Comp. Biochem. Physiol., 61 A, pp. 223-226Sullivan, Oxygenation properties of snake hemoglobin (1967) Science, N.Y., 157, pp. 1308-1310Sullivan, Riggs, The subunits dissociation properties of turtle hemoglobin (1967) Biochim. biophys. Acta, 140, pp. 274-28

Separation And Functional Characterization Of Leptodactylus Labyrinthicus Hemoglobin Components

1. 1. Some functional and structural properties of Leptodactylus labyrinthicus hemoglobin were studied. 2. 2. Three distinct components were isolated by CM-cellulose chromatography corresponding to 10, 60 and 30% of the total hemolysate. 3. 3. The whole hemolysate as well as the major component presented no Bohr effect, although the 30% component exhibited a normal alkaline Bohr effect, and all of them showed an heterotropic effect of phosphates on the oxygen affinity. 4. 4. The globins of the two major components were obtained and their two chains were identified by polyacrylamide gel disc electrophoresis. © 1983.761123125Bertini, Rathe, Electrophoretic analysis of the hemoglobin of various species of anurans (1962) Copeia, 1, pp. 181-185Darlington, The geographical distribution of animals (1957) Zoogeography, pp. 675-687. , Wiley, Sons, Wiley, New YorkHamada, Sakay, Shukuya, Kaziro, Biochemical metamorphosis of hemoglobin in Rana catesbeiana (1964) J. biol. Chem., 55, pp. 636-642MacLean, Jurd, The hemoglobins of healthy and anaemic Xenopus laevis (1971) J. cell. Sci., 9, pp. 509-528Meirelles, Vieira, Airoldi, Focesi, Jr., Some larval properties of Pipa carvalhoi adult hemoglobins (1979) Comp. Biochem. Physiol., 62 A, pp. 859-862Osborn, Weber, The reliability of molecular weight determination by dodecylsulfate-polyacrylamide gel electrophoresis (1969) J. biol. Chem., 16, pp. 4406-4412Riggs, The metamorphosis of hemoglobin in the bullfrog (1951) J. gen. Physiol., 35, pp. 23-40Rossi-Fanelli, Antonini, Studies on the oxygen and carbon monoxide equilibria of human myoglobin (1958) Archs. Biochem. Biophys., 77, pp. 478-492Sullivan, Amphibian hemoglobins (1974) Chemical Zoology, pp. 77-118. , M Florkin, B.T Scheer, Academic Press, New YorkSullivan, Nute, Structural and functional properties of polymorphic hemoglobins from orangutans (1968) Genetics, 58, pp. 113-124Sunderman, Jr., (1964) Hemoglobin, p. 104. , W.F.D Sunderman, W.F Sunderman Jr., Lippincott, Philadelphi

Kinetics Of Oxygen And Carbon Monoxide Binding To The Hemoglobins Of The Water Snakes Liophis Miliaris And Helicops Modestus

1. 1. Liophis miliaris and Helicops modestus are water snakes having different respiratory adaptiations to their specific habitats. L. miliaris is more active and spends more time on land than H. modestus. Knowledge of the equilibrium and kinetics of ligand binding to their hemoglobins leads to better understanding of molecular aspects of this adaptation. 2. 2. Both snakes contain several hemoglobin types in their blood. Studies on the kinetics of oxygen dissociation and carbon monoxide combination with these hemoglobins were performed by stopped-flow and flash-photolysis experiments at various pH values, both in the presence and absence of adenosine triphosphate. 3. 3. The oxygen dissociation kinetics of L. miliaris hemoglobins show a strong pH dependence and cooperative interactions between chains are indicated by autocatalytic time-courses at pH 7.0. In contrast, H. moledstus hemoglobins show nearly pH independent rate constants for oxygen dissociation and cooperative interactions between chains were not apparent. The hemoglobins of H. modestus show increased pH dependence in the presence of adenosine triphosphate. 4. 4. The carbon monoxide combination kinetics differ for the hemoglobins of L. miliaris and H. modestus in general agreement with the differences found in the kinetics and equilibria of oxygen binding. Both the kinetic and steady-state difference between these hemoglobins may be advantageous in light of the behavioral differences of these two water snakes. © 1980.674555559IEEE Intelligent Transportation Systems Society (ITSS)Antonini, Brunori, (1971) Hemoglobin and Myoglobin in Their Reactions with Ligands, , North Holland, AmsterdamBonaventura, Sullivan, Bonaventura, Effects of pH and anions on functional properties of hemoglobin from Lemur fulvus fulvus (1974) J. biol. Chem., 249, pp. 3768-3775Lenfant, Johansen, Torrance, Gas transport and oxygen storage capacity in some pinnipeds and the sea otter (1970) Respiration Physiology, 9, pp. 977-986Ogo, Abe, Focesi, Jr, Oxygen dissociation constants in hemoglobins of Helicops modestus and Liophis miliaris two water-snakes with different morphological adaptations to their aquatic environment (1979) Comp. Biochem. Physiol., 63 A, pp. 285-289Ogo, Focesi, Jr, The hemoglobin Bohr effect and lactic acid content of the blood of two water-snakes with different degrees of aquatic adaptation (1979) Experientia, 35, pp. 862-863Seymor, Webster, Gas transport and blood acid-base balance in diving sea snakes (1975) J. exp. Zool., 191, pp. 169-18

Allosteric Effect Of Protons And Adenosine Triphosphate On Hemoglobins From Aquatic Amphibia

The analysis of hemoglobins from two anurans, one semi-aquatic (Leptodactylus labyrinthicus) and the other aquatic (Pipa carvalhoi), showed several components isolated by CM-cellulose chromatography. The two major components (Hb II and Hb III) of L. labyrinthicus and the major components (Hb III and Hb IV) of P. carvalhoi possess functional properties as follows: i. P. carvalnoi Hb III and Hb IV and L. labyrinthicus Hb II had very small Bohr effects (-0.05) and a substantial heterotropic effect with polyphosphates. ii. L. labyrinthicus Hb III produced a normal Bohr effect of -0.17, with no influence of polyphosphates. © 1985 Springer-Verlag.155335335

Interactions Of Adenosine Triphosphate With Snake Hemoglobins. Studies In Liophis Miliaris, Boa Constrictor And Bothrops Alternatus

The hemoglobins of three snake species: Liophis miliaris, Bothrops alternatus and Boa constrictor present a single ATP binding site per tetramer. The ATP association constant values for the deoxyhemoglobins at pH 7.5 were about KD ≅ 106 M-1 (107 M-1 for B. contrictor), three to four orders of magnitude higher than the respective values for oxyhemoglobin of about KO ≅ 102 M-1. The deoxyhemoglobin constant values markedly decrease as a function of pH, becoming, at pH 8.5, about KD ≅ 103 M-1 whereas for the oxyhemoglobin the constants remain of about the same, KO ≅ 102 M-1, at the pH range studied. The high ATP binding affinity constants, compared to those of human hemoglobin A, were explained from a molecular structural standpoint, considering L. miliaris hemoglobin, whose complete primary sequence is known. Two distinct amino acid residue differences were found in the β-chain, one being Trp (NA3) (more hydrophobic) in the snake hemoglobin which substitutes the Leu (NA3) in human hemoglobin, and the second being Val 101 β (G3) instead of Glu 101 β (G3). The substitutions could provide an un-neutralized, positively charged, residue Lys-104β and, taking into account its high pK value, the pH dependence of ATP binding affinity for the snake hemoglobin would originate from pH-dependent ionization of phosphate groups of the allosteric effector. The physiological implications of the high ATP binding constant, as well as the possible protective role of the nucleotide binding against the effect of high environmental temperatures on the oxygen dissociation curves, are discussed. © 1994.1094701707Ackers, Linked functions in allosteric proteins: an exact theory for the effect of organic phosphates on oxygen affinity of hemoglobin (1979) Biochemistry, 18, pp. 3372-3380Adair, The hemoglobin system—IV. The oxygen dissociation curve of hemoglobin (1925) J. biol. Chem., 63, pp. 529-538Amiconi, Bertollini, Bellelli, Coletta, Condó, Brunori, Evidence for two oxygen-linked binding sites for polyanions indromedary hemoglobin (1985) Eur. J. Biochem., 150, pp. 387-393Antonini, Condó, Giardina, Ioppolo, Bertollini, The effect of pH and d-glycerate-2,3-biphosphate on the O2 equilibrium of normal and SH (β-93) modified human hemoglobin (1982) Eur. J. Biochem., 121, pp. 325-328Bartlett, Phosphate compounds in vertebrate red blood cells (1980) Am. Zool., 20, pp. 103-114Benesch, Edalji, Benesch, The allosteric effect of inositol hexasulfate on oxygen binding by hemoglobin (1976) Biochemistry, 15, pp. 3396-3398Cashon, Bonaventura, Bonaventura, Focesi, Jr, The nicotinamide adenine dinucleotides as allosteric effectors of human hemoglobin (1986) J. biol. Chem., 261, pp. 12700-12705Focesi, Jr, Bonilla, Nagatomo, Matsuura, Dimer-tetramer transition in hemoglobin from Liophis miliaris—III. The phenomenon in snake species of different evolutionary levels (1992) Comp. Biochem. Physiol., 103 B, pp. 985-989Focesi, Jr, Ogo, Matsuura, Dimer-tetramer transition in hemoglobins from Liophis miliaris—II. Evidence with the stripped protein (1990) Comp. Biochem. Physiol., 96 B, pp. 119-122Focesi, Jr, Takagi, Ogo, Polyphosphate binding sites in Liophis miliaris hemoglobin (1990) Evidence with reduced nicotinamide adenine dinucleotide phosphate, 62, pp. 401-408. , Ann. Acad. bras. Ci., (4)Imai, (1992) Allosteric Effects in Haemoglobin, , Cambridge University Press, Cambridge, U.KIslam, Persson, Zaidi, Jornvall, Sea-snake (Microcephalopis gracilis) hemoglobin: primary structure and relationships to other forms (1990) J. Prot. Chem., 9, pp. 533-541McDonald, Turci, Bleichman, Functional and subunit assembly properties of hemoglobin Alberta (α2β2 101Glu→Gly) (1985) J. Mol. Biol., 183, pp. 105-112MacMahon, Hamer, Effect of temperature and photoperiod on oxygenation and other blood parameters of the sidewinder (Crotalus cerastes): adaptative significance (1975) Comp. Biochem. Physiol., 51 A, pp. 59-69Matsuura, Fushitani, Riggs, The amino acid sequences of the α and β chains of hemoglobin from the snake, Liophis miliaris (1989) J. biol. Chem., 264 (10), pp. 5515-5521Matsuura, Ogo, Focesi, Jr, Dimer-tetramer transition in hemoglobins from Liophis miliaris—I. Effect of organic polyphosphate (1987) Comp. Biochem. Physiol., 86 A, pp. 683-687Naqvi, Nadvi, Zaidi, Partial sequence of hemoglobin from cobra (Naja naja naja) (1987) Biosci. Rep., 7, pp. 813-819Ogo, Focesi, Jr, Cashon, Bonaventura, Bonaventura, Interactions of nicotinamide adenine dinucleotides with varied states and forms of hemoglobin (1989) J. Biol. Chem., 264, pp. 11302-11306Oyama, Jr, Nagatomo, Bonilla, Matsuura, Focesi, Jr, Bothrops alternatus hemoglobin components (1993) Oxygen binding properties and globin chain hydrophobic analysis, 105 B, pp. 271-275. , Comp. Biochem. Physiol., (2)Powers, Molecular ecology of Teleost fish hemoglobin: strategies for adapting to changing environment (1980) Am. Zool., 20, pp. 139-162Press, Flannery, Teukolsky, Vetterling, (1986) Numerical Recipes: The Art of Scientific Computing, , Cambridge University Press, Cambridge, U.KRiggs, Wolbach, Sulfhydryl groups and the structure of hemoglobin (1956) The Journal of General Physiology, 39, pp. 585-605Rossi-Fanelli, Antonini, Studies on the oxygen and carbon monoxide equilibria of human hemoglobin (1958) Archs Biochem. Biophys., 77, pp. 478-492Shih, Jones, Imai, Tyuma, Involvement of Glu G3(101)β in the function of hemoglobin (1985) Comparative O2 equilibrium studies of human mutant hemoglobins, 260, pp. 5919-5924. , J. biol. ChemSzabo, Karplus, A mathematical model for structure-function relations in hemoglobin (1972) J. Mol. Biol., 72, pp. 163-197Szabo, Karplus, Analysis of the interaction of organic phosphates with hemoglobin (1976) Biochemistry, 15, pp. 2869-2877Weber, Jensen, Functional adaptation in hemoglobins from ectothermic vertebrates (1988) A. Rev. Physiol., 50, pp. 161-179Wyman, Jr, Linked functions and reciprocal effects in hemoglobin: a second book (1964) Adv. Prot. Chem., 19, pp. 223-28

Dimer-tetramer Transition In Hemoglobin From Liophis Miliaris-iii. The Phenomenon In Snake Species Of Different Evolutionary Levels

1. 1. The primitive snake Boa constrictor presents in the stripped hemolysate one component which from O2, equilibrium curves produced the following values: log P50 ± -0.1 and Hill coefficient nH = 1.1, independent of pH. 2. 2. Bothrops alternatus, an evolved snake, presents two components in the hemolysate with functional parameters: log P50 = 0.4 and nH = 1.7 at pH 7.1, decreasing to log P50 = -0.1 and nH ± 1.4 at pH 8.2. 3. 3. In the presence of ATP, an increase to log P50 ± 0.9 and nH ± 2 is found in both snake hemolysates, up to pH 7.8 4. 4. Molecular weight determinations by gel filtration at pH 8 show only the dimeric form (mol. wt 32,000) in B. constrictor hemolysate, and dimers and tetramers (mol. wt 64,500) in that of B. alternatus. 5. 5. The Hill plots as a function of O2 tension show for B. alternatus hemolysate a shift from deoxytetramer nH = 2.02 to oxydimer nH = 0.88 as occurs in L. miliaris. For B. constrictor hemoglobin the nH remains 1.0 independent of the O(in2) tension. © 1992.1034985989A.d'A, (1970) Reptiles, , Hutchinson and Co. Ltd, LondonBonilla, Estrutura, funçã e evolução em hemoglobinas de ofidios (1992) Ph.D. Dissertation, , Universidade Estadual de Campinas, BrazilFocesi, Jr., Ogo, Bonaventura, Bonaventura, Kinetics of oxygen and carbon monoxide binding to the hemoglobins of the water-snakes Liophis miliaris and Helicops modestus (1980) Comp. Biochem. Physiol., 67 (A), pp. 555-559Focesi, Jr., Ogo, Matsuura, Further evidence of dimer-tetramer transition in hemoglobin from Liophis miliaris (1987) Brazilian J. Med. Biol. Res., 20, pp. 861-864Focesi, Jr., Ogo, Matsuura, Dimer-tetramer transition in hemoglobins from Liophis miliaris—II. Evidence with the stripped protein (1990) Comp. Biochem. Physiol., 96 B, pp. 119-122Matsuura, Fushitani, Riggs, The amino acid sequences of the α and β chains of hemoglobin from the snake, Liophis miliaris (1989) J. biol. Chem., 264 (10), pp. 5515-5521Matsuura, Ogo, Focesi, Jr., Dimer-tetramer transition in hemoglobins from Liophis miliaris—I. Effect of organic polyphosphate (1987) Comp. Biochem. Physiol., 86 A, pp. 683-687Matsuura M. S. A., Rosa J. C., Greene L. J. and Focesi A., Jr., (1992) In preparationMonod, Wyman, Changeaux, On the nature of allosteric transitions: a plausible model (1965) J. Molec. Biol., 12, pp. 88-118Ogo, Abe, Focesi, Jr., Oxygen dissociation constants in hemoglobins of Helicops modestus and Liophis miliaris two water-snakes with different morphological adaptations to their aquatic environment (1979) Comp. Biochem. Physiol., 63 A, pp. 285-289Oyama S., Jr., Bonilla G. O., Matsuura M. S. A. and Focesi A., Jr. (1992) In preparationPope, (1974) The Reptile World: A Natural History of the Snakes, Lizards, Turtles, and Crocodilians, , A. Alfred, 7th edn., Knopf Inc, N.YRossi-Fanelli, Antonini, Studies on the oxygen and carbonmonoxide equilibria of human hemoglobin (1958) Arch. Biochem. Biophys., 77, pp. 478-492Ruben, Aerobic and anaerobic metabolism during activity in snakes (1976) J. comp. Physiol., 109 B, pp. 147-157Schwantes, Schwantes, Bonaventura, Sullivan, Bonaventura, Hemoglobins of Boa constrictor amaralis (1976) Comp. Biochem. Physiol., 54 B, pp. 447-45

Bothrops Alternatus Hemoglobin Components. Oxygen Binding Properties And Globin Chain Hydrophobic Analysis

1. 1. Bothrops alternatus oxyhemolysate showed two components by DE-52 cellulose ion-exchange chromatography and polyacrylamide gel electrophoresis: Hb I representing 70% of the hemolysate and Hb II (30%); both are dimeric in the stripped from (mol.wt 32,500 Da) and tetrameric in the presence of IHP (64,000 Da). 2. 2. Hb I, Hb II and whole hemolysate showed functionally similar properties to those of Liophis miliaris, i.e. for the stripped form over the pH interval 7.2-8.9; log P50 values decreasing from ±0.1 to ± -0.15 (thereby an alkaline Bohr effect); ΔH+ = -0.38 and Hill coefficient values decreasing from nH = 1.5 to 1.0. In the presence of ATP, an abrupt decrease in O2 affinity occurs and the log P50 values change from 1.0 to 0.5; the Bohr effect increases to ΔH+ = -0.7 whereas the nH values decrease from ≥2 to values close to unity. 3. 3. For B. alternatus, at a physiological pH range (7.8-9.0) the hemoglobin Bohr effect becomes apparent only in the presence of ATP and this seems to be fundamental for the O2 uptake of the snake. 4. 4. HPLC analysis of the globins shows eight different chains instead of four, as found in L. miliaris hemoglobin, which corroborates the presence of Hb I and Hb II components in B. alternatus, and also shows that the unique tetramer formed from different α and β chains is also consistent in this snake. © 1993.1052271275Antonini, Brunori, (1971) Hemoglobin and Myoglobin in their Reaction with Ligands, , North-Holland, AmsterdamBartlett, Phosphate compounds in vertebrate red blood cells (1980) Am. Zool., 20, pp. 103-114Bonilla, Estrutura, a funçã e evolução em hemoglobinas de ofidios (1992) Ph.D. Thesis, , Universidade Estadual de Campinas, BrazilDessauer, Fox, Ramirez, Preliminary attempt to correlate paper-electrophoretic migration of hemoglobin with phylogeny in Amphibia and Reptilia (1957) Archs Biochem. Biophys., 71, pp. 11-17Focesi, Jr, Bonilla, Nagatomo, Matsuura, Dimer-tetramer transition in hemoglobin from Liophis miliaris. III. The phenomenon in snake species of different evolutionary levels (1992) Comp. Biochem. Physiol., 103 B, pp. 985-989Focesi, Jr, Ogo, Matsuura, Dimer-tetramer transition in hemoglobins from Liophis miliaris. II. Evidence with the stripped protein (1990) Comp. Biochem. Physiol., 96 B, pp. 119-122Matsuura, Ogo, Focesi, Jr., Dimer-tetramer transition in hemoglobins from Liophis miliaris. I. Effect of organic polyphosphate (1987) Comp. Biochem. Physiol., 86 A, pp. 683-687Matsuura, Fushitani, Riggs, The amino acid sequences of the α and β chains of hemoglobin from the snake, Liophis miliaris (1989) J. biol. Chem., 264, pp. 5515-5521Matsuura, Rosa, Greene, Focesi, Jr, Amino acid sequence of the β-chain of heuroglobin from the snake Liophin miliaris (1992) FASEB J., 6 (1), p. AS7Monod, Wyman, Changeaux, On the nature of allosteric transitions: a plausible model (1965) J. molec. Biol., 12, pp. 88-118Ornstein, Disc electrophoresis background and theory (1964) Ann. N.Y. Acad. Sci., 121, pp. 321-349Rossi-Fanelli, Antonini, Studies on the oxygen and carbon-monoxide equilibria of human hemoglobin (1958) Archs Biochem. Biophys., 77, pp. 478-492Schwantes, Hemoglobinas e haptoglobinas em serpentes (1972) Ph.D Thesis, , Universidade Federal do Rio Grande do Sul, BrasilSode, Oxygen binding characteristic of whole-blood and hemoglobin from the snake Thamnophis sirtalis (1991) Comp. Biochem. Physiol., 100 B, pp. 697-703Sullivan, Reptilian hemoglobins (1974) Chemical Zoology, 9, pp. 377-398. , M. Florkin, B.T. Scheer, Academic Press, New York, Amphibia and Reptili

Functional Properties Of Aplysia Brasiliana Myoglobin

1. 1. The radular myoglobin of the Brazilian sea hare, Aplysia brasiliana, has been isolated and its ligand binding properties have been characterized. The myoglobin is similar to the myoglobin of Aplysia limacina (a Mediterranean species), and has a lower oxygen affinity than does myoglobin of the sperm whale, Physeter macrocephalus. 2. 2. Aplysia brasiliana myoglobin is a monomer and binds oxygen and other heme ligands non-cooperatively. There is no evidence of pH sensitivity in these processes. 3. 3. The kinetics of ligand binding and dissociation are simple processes. The lower oxygen affinity of Aplysia brasiliana myoglobin relative to sperm whale myoglobin is associated with a much higher rate of oxygen dissociation, with first order rate constants of 125 sec-1 and 10 sec-1 respectively. © 1978.612223226Anderson, Brunori, Weber, Fluorescence studies of Aplysia and sperm whale apomyoglobins (1970) Biochemistry, 24, pp. 4723-4729Antonini, Brunori, (1971) Hemoglobin and Myoglobin in their Reactions with Ligands, , North Holland, AmsterdamBlundell, Brunori, Curti, Bolognesi, Coda, Fumagalli, Ungaretti, Crystallization and preliminary X-ray diffraction studies on met-myoglobin from Aplysia limacina (1975) J. molec. Biol., 97, pp. 665-666Bonaventura, Sullivan, Bonaventura, Effects of pH and anions on functional properties of hemoglobin from Lemur fulvus fulvus (1974) J. blol. Chem., 249, pp. 3768-3775Brunori, Antonini, Fasella, Wyman, Fanelli, Reversible thermal denaturation of Aplysia myoglobin (1968) J. molec. Biol., 34, pp. 497-504Brunori, Ughetta, Rotilio, Antonini, Wyman, Redox equilibrium of sperm-whale myoglobin, Aplysia myoglobin, and Chironomus thummi hemoglobin (1971) Biochemistry, 10, pp. 1604-1609Brunori, Giacometti, Antonini, Wyman, Denaturation of Aplysia myoglobin. Equilibrium study (1972) J. molec. Biol., 63, pp. 139-152Giacometti, Da Ros, Antonini, Brunori, Equilibrium and kinetics of the reaction of Aplysia myoglobin with azide (1975) Biochemistry, 14, pp. 1584-1588Guiseppe, Calabrese, Giacometti, Brunori, An electron paramagnetic resonance study of Aplysia myoglobin (1971) Biochimica et Biophysica Acta (BBA) - Protein Structure, 236, pp. 234-237Perutz, Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 Å resolution: (1) X-ray analysis (1968) Nature, Lond., 219, pp. 29-32Riggs, Wolbach, Sulphydryl groups and the structure of hemoglobin (1956) The Journal of General Physiology, 39, pp. 585-605Rossi-Fanelli, Antonini, A new type of myoglobin isolated and crystallized from the muscles of Aplysiae (1957) Biochemia (URSS), 22, pp. 344-355Rossi-Fanelli, Antonini, Povoledo, Further study on myoglobin II. Chemical and biochemical properties of a new type of myoglobin in molluscs, in Neuberger, A (1960) Symposium on Protein Structure, pp. 143-147. , Methuen, LondonSekino, Ogo, Montouchet, Focesi, Jr., Denaturation of Aplysia brasiliana myoglobin (1976) Tenth International Congress of Biochemistry, p. 169. , Abstract volumeTakano, Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of metmyoglobin for sperm whale (1977) J. molec. Biol., 110, pp. 537-568Takano, Structure of myoglobin refined at 2.0 Å resolution. II. Structure of deoxymyoglobin from sperm whale (1977) J. molec. Biol., 110, pp. 569-584Tentori, Vivaldi, Carta, Marinucci, Massa, Antonini, Brunori, Amino acid sequence of Aplysia limacina myoglobin (1973) Int. J. Peptide Protein Res., 5, pp. 187-200Wittenberg, Brunori, Wittenberg, Wyman, Kinetics of the reactions of Aplysia myoglobin with oxygen and carbon monoxide (1965) Archs Biochem. Biophys., 111, pp. 576-57

Separation And Characterization Of The Hemoglobin Components Of Pterygoplichthys Pardalis, The Acaribodo

1. 1. The four main hemoglobin components of the hemolysate of Pterygoplichthys pardalis have been isolated and characterized. 2. 2. The functional properties investigated for the isolated components comprise the effect of pH and ATP on (i) the O2 equilibrium, (ii) the O2 dissociation kinetics, (iii) the CO combination kinetics. 3. 3. Component I, corresponding to approx 50% of the total hemoglobin, is characterized by functional properties which are distinctly different from those of Components II, III and IV, which are alike 4. 4. Thus it is shown, once more, that multiple components in an hemolysate fall into categories of hemoglobins characterized by distinct and complementary functional properties. © 1979.621173177IEEE Communications Society,IEEE Computer SocietyAntonini, Brunori, (1971) Hemoglobin and Myoglobin in their Reactions with Ligands, , North-Holland, AmsterdamBrunori, Molecular adaptation to physiological requirements (1975) Curr. Top. Cell. Regulation, 9, pp. 1-39Brunori, Giardina, Antonini, Benedetti, Bianchini, (1974) J. molec. Biol., 86, pp. 165-169Bunn, Riggs, The measurement of the Bohr effect of fish hemoglobins by gel electrofocusing (1979) Comp. Biochem. Physiol., 62 A, pp. 95-100Fink, Fink, Central Amazonia and its fishes (1979) Comp. Biochem. Physiol., 62 A, pp. 13-30Fyhn, Fyhn, Davis, Powers, Fink, Garlick, Hemoglobin heterogeneity in Amazonian fishes (1979) Comp. Biochem. Physiol., 62 A, pp. 39-66Greenwood, Rosen, Weitzman, Myers, Phyletic studies of Teleostean fishes with a provisional classification of living forms (1966) Bull. Am. Mus. Nat. Hist., 131, pp. 339-455Martin, Bonaventura, Brunori, Fyhn, Fyhn, Garkick, Powers, Wilson, The isolation and characterization of the hemoglobin components ofMylossoma sp., an Amazonian teleost (1979) Comp. Biochem. Physiol., 62 A, pp. 155-162Riggs, Wolbach, Sulfhydryl groups and the structure of hemoglobin (1956) The Journal of General Physiology, 39, pp. 585-605Washburn, (1926) International Critical Tables of Numerical Data, Physics, Chemistry and TechnologyWeber, Wood, Effects of erythrocyte nucleoside triphosphates on oxygen equilibria of composite and fractionated hemoglobins from the facultative air-breathing Amazonian Catfish,Hypostomus andPterygoplichthys (1978) Comp. Biochem. Physiol., 62 A, pp. 179-18