Oxygen Binding Properties Of Erythrocruorin Solution And Blood Ph Of The Giant Earthworm Glossoscolex Paulistus (oligochaeta, Glossoscolecidae)

1. 1. The oxygen affinity of Glossoscolex paulistus erythrocruorin solution increased concurrently with pH, from 5.8 to 2.4 torr over the pH range 7.0-8.0. P50 values were in the range hitherto reported for the Oligochaeta. 2. 2. Blood pH varied from 7.27 to 7.40 (mean = 7.32) at 20°C in anesthetized earthworms. 3. 3. The Bohr effect was dependent on the pH range studied, and varied from -0.05 to -1.7. At the blood pH recorded the calculated Bohr effect was -0.46. © 1985.8015355Cordero, Oligoquetos sudamericanos de la familia Glossoscolecidäe, VI. Los generos de la subfamilia Glossoscolecinae, sus probables relaciones fileticas y su distribucicion geografica actual (1945) Comun. Zool. Mus. Hist. Nat. Montevideo, 1 (22), pp. 1-28Cosgrove, Schwartz, The properties and function of the blood pigment of the earthworm (1965) Lumbricus terrestris. Physiol. Zool., 38, pp. 206-212Dales, Respiration and energy metabolism in annelids (1969) Chemical Zoology, Annelida, Echiura, Sipuncula, 4, pp. 93-109. , M Florkin, B.T Scheer, Academic Press, LondonHack, An application of a method of gas microanalysis to the study of soil air (1956) Soil Science, 182, pp. 217-232Haughton, Kerkut, Munday, The oxygen dissociation and alkaline denaturation of haemoglobins from two species of earthworm (1958) J. exp. Biol., 35, pp. 360-368Howell, Rahn, Goodfellow, Herreid, Acid-base regulation and temperature in selected invertebrates as a function of temperature (1973) Am. Zool., 13, pp. 557-563Johansen, Martin, Circulation in a giant earthworm, Glossoscolex giganteus (1966) J. exp. Biol., 45, pp. 165-172Jordan, Schwartz, Einfache Apparate zur Gasanalyse und Mikrorespirometrie in bestimmten Gasgemishen, und über die Bedeutung des Hämoglobins beim Regenwurm (1920) Pflügers Arch., 185, pp. 311-321Mangum, Schick, The pH of body fluids of marine invertebrates (1972) Comp. Biochem. Physiol., 42 A, pp. 693-697Mangum, Likkebue, Johansen, Oxygen uptake and the role of hemoglobin in the East African swanpworm, Alma emini (1975) Comp. Biochem. Physiol., 52 A, pp. 477-482Manwell, Oxygen equilibrium of Phascolosoma agassizzi hemerythrin (1958) Science, 127, pp. 592-593Marks, Stein, Cooper, Acid phosphatase changes associated with response to foreign tissue in the earthworm Lumbricus terrestris (1981) Comp. Biochem. Physiol., 68 A, pp. 681-683Mendes, Nonato, The respiratory metabolism of tropical earthworms. II. Studies on cutaneous respiration (1957) Bol. Fac. Fil., Clê. Letr. Univ. São Paulo, Zool., 21, pp. 153-166Mendes, Valente, The respiratory metabolism of tropical earthworms. I. The respiratory rate and the action of carbon monoxide at normal oxygen pressure (1953) Bol. Fac. Fil., Ciê. Letr. Univ. São Paulo, Zool., 18, pp. 91-102Righi, Bionomic considerations upon the Glossoscolecidae (Oligochaeta) (1972) Pedobiologia, 12, pp. 254-260Righi, Sobre a família Glossoscolecidae (Oligochaeta) no Brasil (1972) Arquivos de Zoologia, 20, pp. 1-95Righi, Topography of circulatory system of Glossoscolex paulistus Michaelsen 1926 (Oligochaeta Glossoscolecidae) (1972) Monitore Zool. Ital., 6, pp. 19-36Rossi-Fanelli, Antonini, Studies on the oxygen and carbon monoxide equilibria of human myoglobin (1958) Archs Biochem. Biophys., 77, pp. 478-492Rossi-Fanelli, Chiancone, Vecchini, Antonini, Studies on erythrocruorin I Physicochemical properties of earthworm erythrocruorin (1970) Archives of Biochemistry and Biophysics, 141, pp. 278-283Svedberg, Eriksson, The molecular weight of erythrocruorin (1933) J. Am. Chem. Soc., 55, pp. 2834-2841Truchot, Temperature and acid-base regulation in the shore crab Carcinus maenas (L) (1973) Respiration Physiology, 17, pp. 11-20Weber, Respiratory pigments (1978) Physiology of Annelids, pp. 393-1345. , P.J Mill, Academic Press, LondonWells, Hydrogen ion activity in polychaete body fluids (1974) Comp. Biochem. Physiol., 49 A, pp. 567-57

Erythrocruorin Of Glossoscolex Paulistus (righi) (oligochaeta, Glossoscolecidae): Effects Of Divalent Ions, Acid-alkaline Transition And Alkali And Urea Denaturation

The oxygen affinity and cooperativity of erythrocruorin of Glossoscolex paulistus were studied as a function of cation concentration (Ca2+, Mg2+ and Mn2+). Acid-alkaline transition showed the presence of population multiplicity. Differences in t 1 2 values were observed for native and dissociated forms when submitted to alkaline medium. Urea 6.0-8.0 M caused modifications of the protein structure. © 1995.1112311318Abe, Meirelles, Oxygen binding properties of erythrocruorin and blood pH of the giant earthworm Glossoscolex paulistus (Oligochaeta, Glossoscolecidae) (1985) Comp. Biochem. Physiol., 80, pp. 53-55Antonini, Brunori, (1971) Haemoglobin and Myo-globin in Their Reactions with Ligands, , North-Holland, AmsterdamCaracelli, Meirelles, Tabak, Baffa Filho, Nascimento, An ESR study of nitrosyl—Aplysia brasiliana myoglobin and nitrosyl annelidae Glossoscolex paulistus erythrocruorin (1988) Biochim. Biophys. Acta, 955, pp. 315-320Costa, Bonafé, Meirelles, Galembeck, Sedimentation coefficient and minimum molecular weight of extracellular hemoglobin of Glossoscolex paulistus (Oligochaeta, Glossocolecidae) (1988) Brazilian J. Med. Biol. Res., 21, pp. 115-118Desideri, Verzili, Ascoli, Chiancone, Antonini, High and low-spin EPR forms of the ferric derivative of earthworm erythrocruorin (1982) Biochim. Biophys. Acta, 708, pp. 1-5Fushitani, Imai, Riggs, Oxygenation properties of hemoglobin from the earthworm Lumbricus terrestris (1986) J. biol. Chem., 261, pp. 8414-8423Giardina, Chiancone, Antonini, Studies on erythrocruorin III. Oxygen equilibrium of earthworm erythrocruorin (1975) J. mol. Biol., 93, pp. 1-10Haeser, Datadi, Petersen, Ulha-Cintra, Sawaya, Chemical studies on the giant earthworm Glossoscolex giganteus (Leuckart) (1965) Comparative Biochemistry and Physiology, 16, pp. 491-496Haughton, Kerkut, Munday, The oxygen dissociation and alkaline denaturation of haemoglobins from two species of earthworm (1958) J. exp. Biol., 35, pp. 360-368Igarashi, Kimura, Kajita, Analysis of oxygen equilibria of the giant hemoglobin from the earthworm Eisenia foetida using the Adair Model (1986) J. Biochem., 109, pp. 256-261Meirelles, Oliveira, De Paula, Marangoni, Marques, Erythrocruorin of Glossoscolex paulistus (Oligochaeta, Glossoscolecidae): presence of disulfide bonds and their relation to ligand properties (1985) Comp. Biochem. Physiol., 82 B, pp. 203-205Meirelles, Oliveira, Oliveira, De Paula, Marangoni, Rennebeck, Erythro-cruorin of Glossoscolex paulistus (Oligochaeta, Glosso-scolecidae): dissociation at alkaline pH and its ligands properties as revealed by chemical, immunochemical and electron micoscopy studies (1987) Comp. Biochem. Physiol., 88 A, pp. 377-379Ochiai, Dissociation and oxygen equilibrium properties of the earthworm (Pheretima hilgendorfi) hemoglobin (1983) Arch. Biochem. Biophys., 226, pp. 111-117Ochiai, Dissociation and oxygen equilibrium properties of the extracellular hemoglobin of Eisenia foetida (1984) Arch. Biochem. Biophys., 231, pp. 136-143Perussi, Imasato, Tabak, Meirelles, Fluorescence study of the extracellular hemoglobin of Glossoscolex paulistus erythrocruorin (1990) Phys. Chem. Phys. Med. NMR, 22, pp. 159-168Perussi, Souza, Tinto, Imasato, Meirelles, Tabak, Oxidation of the extracellular hemoglobin of Glossoscolex paulistus (1990) Invertebrate Oxygen Carriers, , S. Vinogradov, O. Kapp, Springer, BerlinShortle, Meeker, Gerring, Effects of denaturants and low concentration on the reversible denaturation of Staphylococcal nuclease (1989) Arch. Biochem. Biophys., 272, pp. 103-113Silva, Villas-Boas, Bonafé, Meirelles, Anomalous pressure dissociation of large protein aggregates (1989) J. biol. Chem., 264, pp. 15863-15868Tsuneshige, Imai, Hori, Tyuma, Gotoh, Spectrophotometric, electron paramagnetic resonance and oxygen binding studies on the hemoglobin from the marine polychaete Perinereis aibuhitensis (Grube): comparative physiology of hemoglobin (1989) J. Biochem., 106, pp. 406-417Vinogradov, Shlom, Kapp, Frossard, The dissociation of annelid extracellular hemoglobins and their quaternary structure (1980) Comp. Biochem. Physiol., 67 B, pp. 1-16Weber, Functions on invertebrate hemoglobins with special reference to adaptation to environmental hypoxia (1980) Am. Zool., 20, pp. 79-101Weber, Cationic control of O2 affinity in lugworm erythrocruorin (1981) Nature, 292, pp. 386-38

6,7-dimethoxy-l-veratrylisoquinoline Alters The Oxygen Dissociation Properties Of Human Hemoglobin: An Esr Study

[No abstract available]9439940

Stratum Corneum Intercellular Lipid As Compared To Erythrocyte Ghosts: An Esr Study Of Thermotropic Behavior And Nitroxide Reduction. Electron Spin Resonance.

Intercellular membranes of Stratum Corneum and erythrocyte ghosts were studied through partition of Tempo nitroxide spin label. Stratum Corneum presents a phase transition-monitored by the spin label at 58 degrees C--that is in agreement with data obtained through the use of other techniques. A reduction of the nitroxide is observed. Erythrocyte ghosts at protein concentrations higher than the values generally used in ESR studies (above 15 mg/ml) also show the partition and reduction of Tempo. Experimental data suggest that the reduction mechanism might be common to both types of membranes involving probably the membrane lipoperoxidation as well as protein oxidation.271637

Mouse Liver Microsomes (mlm) Protect Erythrocytes Against Trifluoperazine (tfp) Induced And Mechanical Hemolysis Which Are Due To Tfp Microsomal Transformation And To The Action Of An Unidentified Water-soluble Microsomal Factor (uf)

Trifluoperazine (TFP), a phenothiazine derivative, produces either hemolysis or protection of erythrocytes under isosmotic conditions in a dose-dependent manner. The hemolytic effect of TFP is abolished in the presence of mouse liver microsomes (MLM) which is due, in part, to drug incorporation, transformation and a MLM enzyme driven metabolism. An unidentified water-soluble factor (or factors) derived from MLM has been found to protect erythrocytes against both mechanical and TFP-induced isosmotic hemolysis.19434935

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

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

Effect Of 1-(p-methoxybenzyl)-6,7-methylenedioxyisoquinoline On Mitochondrial Respiration

[No abstract available]271015051507Vercesi, Magalhaes, Meirelles, (1975) ICRS Medical Sci., 3, p. 492Papa, de Gomez-Puyou, Gómez-Puyou, (1975) Eur. J. Biochem., 55, p. 1Lotina, Gómez-Puyou, Tuena de Gómez-Puyou, Chavez, (1973) Archs Biochem. Biophys., 159, p. 517Peña, Chavez, Carabez, Tuena de Gómez-Puyou, (1977) Archs Biochem. Biophys., 180, p. 522Sumner, (1944) Science, N.Y., 100, p. 413Ernster, Dallner, Azzone, (1963) J. biol. Chem., 238, p. 1124Burgos, Redfearn, The inhibition of mitochondrial reduced nicotinamide-adenine dinucleotide oxidation by rotenoids (1965) Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 110, p. 475Gutman, Singer, Casida, (1970) J. biol. Chem., 245, p. 1992Pressman, (1963) J. biol. Chem., 238, p. 401Carafoli, (1974) Biochem. Soc. Symp., 39, p. 8