DOCSLIB.ORG

The Universal Respiratory Pigment

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
The Universal Respiratory Pigment Histol Histopath (1989) 4: 509-51 4 Histology and Histopathology Invited Re vie W The phylogenetic odyssey of the erythrocyte. I Hemoglobin: the universal respiratory pigment Chester A. Glomski and Judith Tamburlin Department of Anatomical Sciences, State University of New York at Buffalo, New York, USA Summary. Hemoglobin is a molecular entity that is Discussion capable of reversibly binding and releasing oxygen in either extra- or intracellular milieus. It is present in The hemoglobin molecule is truly ancient and has scattered invertebrates in physical solution or in cellular been extant for millenia. It has a long evolutionary sites while in vertebrates it is universally located in history and in fact can be viewed as a molecular clock. It circulating erythrocytes. These cells serve as the vehicle has been used to date the separation of the vertebrates for and otherwise foster the optimum utilization hemo- and invertebrates some 1000 million years ago. The globin. Hernoglobin's variable sphere of respiratory emergence of a vertebrate hemoglobin molecule with activities can be viewed as reflecting the specific differing alpha and beta globin chains occurred 500-600 requirements for each organism in which it is observed. million years later. Hemoglobin has persisted since those Once these concepts have been established and the primordial events and has become established as the advantages and limitations of its cytologic packaging single, dominant, essentially universal respiratory recognized, the study of the erythrocyte as expressed in pigment of the vertebrates. By definition respiratory its dimensions, colligative aspects, geometry, internal pigments, of which hemoglobin is the prime represen- morphology and pathologic variations can be approached tative, are inherently pigmented metallo-proteins having in a purposeful manner. the unique ability of reversible binding with oxygen. Although other phylogenetically transitory respiratory Key words: Hemoglobin, Erythrocyte, Comparative molecules have appeared in the invertebrates (e.g. hematology, Respiratory pigments hemocyanin, chlorocruorin) none have approached the importance of hernoglobin. It has become increasingly apparent that hemoglobin enjoys a remarkably broad Introduction biological distribution. It is identifiable in some bacteria, occasional molds, some single celled animals (e.g. the The erythrocyte, by far the most numerous cell in the ciliated protozoans Paramecium caudatum and circulating blood, is the major carrier of oxygen in man Tetrahymena pyriformis) , scattered invertebrates, and all other vertebrates. This cell is uniquely adapted essentially all vertebrates and most surprisingly in the for this function by its high content of an iron-bearing, plant kingdom. This molecule has been identified in the oxygen binding protein, hemoglobin. An understanding nitrogen fixing nodules on the roots of some legumunous of the red cell's functional and pathologic activities in plants as soy bean plants and alfalfa as well as in the non- man (as well as in other vertebrates) can be approached nodulating plant Trema tomentosa. Indeed, recent by first assessing the phylogenetic expression and isolation of the hemoglobin gene from plant root cells has variation in activity of its respiratory pigment. This suggested that hemoglobin genes, inherited from an establishes a basis for an enhanced, continued study and ancestor common to plants and animals, might be deeper understanding of this cell. Hemoglobin is central present in all plants. All aerobic organisms are capable of to the biology of the erythrocyte. synthesizing catalysts such as the heme-containing cytochromes. Consequently they can be viewed as potential carriers of the heme moiety of hemoglobin. Offprint requests to: Dr. Chester A. Glomski, M.D., Ph.D., Department The limiting factor in the appearance of hemoglobin of Anatomical Sciences, State University of New York at Buffalo, apparently lies in the evolved ability to synthesize the Buffalo, New York 14214, U.S.A. highly specific proteins (globins) which when linked with Erythrocyte odyssey into a tetramer composed of two alpha and beta protein units. Thi\ developmental process is believed to have occurred after the evolution ol the jawless fish (e.g. lamprey ancl hagfish) which do not demonstratc heterogeneous hemoglobins composecl of pairs of differing globin chains but before the cartilaginous fish (sharks) and all other vertebrates which do manifest this progression. The evolutionary ascendancc to polymeric hemoglobins can bc appreciated when viewed in light of Alfalfa, a the benefits that are obtainable by legumumus polymeric as opposed to monomeric plant forms. The oxygenation of one heme in an oligomeric hemoglobin molecule, for example, subsequently permits an adjacent fellow heme to bind oxygen with Partial Pressure 0, (mm Hg) greater facility. This alteration in binding affinity, 1 termed heme-heme interaction Fig. 1. Typ~cal s~gmo~dhemoglob~n oxygen d~ssoc~at~oncurve or cooperativity, is due to small (human hernoglobin). The Bohr effect is also ~llustrated.Note the changes in the three dimensional progressive shift of the dissociation curve to the right with a structure of the molecule. An decrease in pH. After VanSlyke and Peters. extension of this enhancement is the observation that all heme establish the constraints of its remarkable property hemoglobin molecules in a of reversible binding and release of oxygen. solution or within an erythrocyte The simplest molecular configuration of hemoglobin become equally oxygenated consists of one heme prosthetic group (a porphyrin ring when exposed to a given volume complexed with a single atom of iron) attached to one of oxygen; e.g. if a solution of globin chain approximately 150 amino acids in length. human (tetrameric) hemoglobin The molecular weight is approximately 17,000 daltons. is 50% saturated with oxygen all Hemoglobins of this order can be found in the free of the molecules will have two coelomocytes of some annelids (multisegmented Representative polychaete oxygenated ferrous atoms. This worms), the larva of the insect Chironomous and in some annelid (multisegmented characteristic also leads to sea cucumbers. The molecular weights of the primitive marine worm) the establishment of the well (invertebrate) hemoglobins that exist free in solution recognized sigmoid hemoglobin oxygen dissociation conversely, tend to be markedly greater and frequently curve which is ideally suited for taking up and release of approach three million daltons as a result of a high oxygen under different conditions (Fig. 1). Monomeric degree of polymerization. Their large molecular dimen- hemoglobins, in contradistinction, usually have hyperbolic sions serve to prevent them from diffusing out of the dissociation curves. The heme moiety of the molecule plasma into the tissues. Most intracellular invertebrate can be considered evolutionarily stable and responsible hemoglobins are monomers or dimers of the basic for the reversible binding of oxygen while the globin is molecular model although tetramers and larger forms structurally variable and through this variation determines can be represented. The characteristic the conditions under which oxygen binding and release tetrameric molecule of vertebrates will be favored (CO,, temperature, oxygen tension, (including man) most likely arose by organic phosphate and inorganic ion levels etc.). the joining of two dimers. The Hemoglobin molecules can therefore be viewed as vertebrates, with the exception of the cctailor made,, for specific species and temporal jawless fish (Agnatha. cyclostomes), all requisites. Man himself demonstrates at least four have a more complex, tetrameric different hemoglobins hemoglobin containing two pairs of during his existence. dissimilar (alpha and beta) globin the Gower I and 'k&~??%wd* chains; it has an average molecular I1 hemoglobins of .&+;4$$:$$;ifGf;ii%a$ weight of 68,000. It has been concluded ;4(r early embryonic life. ' .&%&2"@-4.,> that the original primitive vertebrate fetal and adult Parameoum hemoglobin consisted of four heme hemoglobins. Thc caudatum, a units and four identical polypeptide bRepresentative Sea Cucumber, chicken protozoan chains; it evolved by gene duplication multiple hemoglobins a holothurian Erythrocyte odyssey during its lifetime (hemoglobins P, E, D, A and H) while interpreted as the net result of its fetal and adult hemoglobins are commonplace among two major functions, the loading mammalians. The maturation of a tadpole to a frog is and unloading of oxygen. The similarly associated with a molecular change of its effects of ambient organismnl hemoglobin. Some fish concomitantly manifest two conditions upon hemoglobin at the types of hemoglobin, one highly sensitive to acid pH and oxygen-rich side of the cyelc j one that is acid-insensitive. Certain representatives of (interface with air or water at the, the annelids and molluscs (bivalves or clams) that have gills, lungs, etc.) and the physiologic erythrocytes demonstrate the simultaneous existence of circumstances at the oxygen-pool- mono- and polymeric intracellular hemoglobins. The (tissue) side have to be both taken arcid clam Noetia ponderosa (a colloquial .blood clamn) into balanced consideration. Thu\. possesses erythrocytes with two dimeric hemoglobins fish with both acid sensitive an(l with own ou\cen-binding properties. It can be acid independent hemoglobins (e.g. ~i'ilna, iiaina gi,~;,,,~ assumed that each rainbow trout, Salmo irideus,)
Load more

Recommended publications
  • Teresa Haigh Thesis Submitted for the Degree of Doctor of Philosophy
    r DIELECTROPHORETIC INVESTIGATIONS OF HAEMATOLOGICAL CELLS PROCEDURES AND APPLICATIONS Teresa Haigh Thesis submitted for the degree of Doctor of Philosophy University of York Department of Biology March 1995 DEDICATION This thesis is dedicated to my family and friends for all their support. 11 ABSTRACT The dielectrophoretic phenomenondescribes the translationalmotion of a particle such as a biological cell, in responseto a non-uniform electric field. Both the magnitude and the direction of the induced movementare dependentupon the electrical properties of the cell with respectto its surroundingsand thus are a function of cell composition, and vary according to the alternation frequency of the electric field. Quantification of the responsein terms of the number of cells which exhibit positive dielectrophoretic behaviour, i. e. towards greatestfield intensity, as a function of field frequency,enables characteristicspectra to be compiled. Exploitation of a dielectrophoretic technique for biological analysis offers several advantages; notably that measurements are non-invasive and require no pre- modification of the cell, thus potentially permitting the separation of populations of viable cells. The clinical applications of this phenomena have to date been restricted, since methods for investigating dielectrophoretic response have relied upon manual quantification and been limited by cell sample size. Such difficulties have been minimised by the development of automated detection and analysis systems, enabling a typical collection spectra to be generated within an hour. The development of a dielectrophoretic technique for rapid analysis of haematological cells has been described. A computer-based system was used to control voltage application to a micro-electrode chamber through which a cell suspension was circulated.
    [Show full text]
  • Questioning the Functional Relevance of Mitochondrial Supercomplexes by Time-Resolved Analysis of the Respiratory Chain
    Questioning the functional relevance of mitochondrial PNAS PLUS supercomplexes by time-resolved analysis of the respiratory chain Martin Trouillarda, Brigitte Meunierb, and Fabrice Rappaporta,1 aInstitut de Biologie Physico-Chimique, Unité Mixte de Recherche 7141 Centre National de la Recherche Scientifique-Univ P et M Curie, 13 rue P et M Curie, 75005 Paris, France; and bCentre de Génétique Moléculaire, Unité Propre de Recherche 3404 Centre National de la Recherche Scientifique, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France Edited by Marten Wikstrom, University of Helsinki, Helsinki, Finland, and accepted by the Editorial Board September 19, 2011 (received for review June 13, 2011) Mitochondria are the powerhouses of eukaryotic cells as they feed zation. Since then, many supercomplex assemblies from a wide metabolism with its major substrate. Oxidative-phosphorylation variety of organisms or organs have been biochemically charac- relies on the generation, by an electron/proton transfer chain, of terized, with a large diversity of stoichiometries and complex an electrochemical transmembrane potential utilized to synthesize compositions [see e.g., the recent exhaustive review by Lenaz and ATP. Although these fundamental principles are not a matter of Genova (11)]. This culminated in the isolation by Acin-Pérez, debate, the emerging picture of the respiratory chain diverges et al. of a functional “respirasome” from mammal cells, transfer- from the linear and fluid scheme. Indeed, a growing number of ring electrons all the way from NADH or succinate to molecular pieces of evidence point to membrane compartments that possibly oxygen (12). In addition, the composition and abundance of the restrict the diffusion of electron carriers, and to supramolecular biochemically characterized supercomplexes have been shown to assembly of various complexes within various kinds of super- vary with growth or physiological conditions (13, 14), supporting complexes that modulate the thermodynamic and kinetic proper- their physiological significance.
    [Show full text]
  • Journal Ofbiotechnology
    Journal of Biotechnology 187 (2014) 1–9 Contents lists available at ScienceDirect Journal of Biotechnology journal homepage: www.elsevier.com/locate/jbiotec In vivo biodistribution and oxygenation potential of a new generation of oxygen carrier Tony Le Gall a,b, Valérie Polard c, Morgane Rousselot c, Auréline Lotte c, Mouna Raouane d, Pierre Lehn a,b, Paule Opolon e, Elisabeth Leize f, Eric Deutsch d, Franck Zal c, Tristan Montier a,b,g,∗ a Unité INSERM 1078, SFR 148 ScInBioS, Université de Bretagne Occidentale, Université Européenne de Bretagne, 46 rue Félix Le Dantec, CS51819, 29218 Brest Cedex 02, France b Plateforme SynNanoVect, SFR 148 ScInBioS, Université de Bretagne Occidentale, Faculté de Médecine, 22 rue Camille Desmoulins, 29200 Brest, France c HEMARINA SA, Aéropôle centre, Biotechnopôle, 29600 Morlaix, France d Unité INSERM 1030, Radiothérapie Moléculaire, Université Paris XI, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94805 Villejuif, France e Unité de Pathologie Expérimentale, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94805 Villejuif, France f CHRU de Brest, Département de Prothèses, UFR Odontologie, Brest F29238, France g DUMG, Université de Bretagne Occidentale, CHRU de Brest, service de biochimie et de pharmaco-toxicologie, 5 avenue du Maréchal Foch, 29200 Brest, France article info a b s t r a c t Article history: Natural giant extracellular hemoglobins (Hbs) from polychaete annelids are currently actively inves- Received 3 October 2013 tigated as promising oxygen carriers. Their powerful oxygenating ability and their safety have been Received in revised form 4 July 2014 demonstrated in preclinical studies, motivating their development for therapeutic and industrial applica- Accepted 7 July 2014 tions.
    [Show full text]
  • Biochemical Responses in Penaeids Caused by Contaminants
    Aquaculture 191Ž. 2000 163±168 www.elsevier.nlrlocateraqua-online Biochemical responses in penaeids caused by contaminants Afonso Celso Dias Bainy ) Departamento de Bioquõmica,ÂàCentro de Ciencias Biologicas, UniÕersidade Federal de Santa Catarina, Florianopolis, SC, 88040-900 Brazil Received 1 March 2000; accepted 9 May 2000 Abstract The shrimp aquaculture industry has become increasingly aware of the need for developing sensitive and precise diagnostic toolsŽ. Biomarkers with predictive capability for assessing the toxic effect of commonly encountered chemicals on shrimp culture. Potentially damaging com- pounds used in shrimp culture include disinfectants, therapeutics, feed additives, algicidals, pesticides, and fertilizers. These chemicals may cause biological damage at all life stages during shrimp production. Since many chemicals may be stressors to the organisms, lower production rates may occur, compromising the sustainability of the shrimp production. This manuscript gives a brief overview about toxic effects associated with the chemicals used directly or indirectly during shrimp production. q 2000 Elsevier Science B.V. All rights reserved. Keywords: Penaeid; Biomarker; Contamination 1. Introduction In many countries, the consumption of shrimps has grown yearly but the natural stocks of these decapod crustaceans have been intensively depleted. Alternatively, shrimp culture has been adopted and consolidated as one of the largest profitable aquaculture activities all over the world. Methods of shrimp cultivation adopted by the shrimp aquaculture companies vary from intensive farming to extensive rearing systems. The former requires auxiliary inputs and capital, while the second is to a great extent dependent on natural processes ) Tel.: q55-48-3316561; fax: q55-48-3319672. E-mail address: [email protected]Ž.
    [Show full text]
  • Part 4 Functional Biochemistry
    МІНІСТЕРСТВО ОХОРОНИ ЗДОРОВ'Я УКРАЇНИ Харківський національний медичний університет PART 4 FUNCTIONAL BIOCHEMISTRY Self-Study Guide for Students of General Medicine Faculty in Biochemistry ЧАСТИНА 4 ФУНКЦІОНАЛЬНА БІОХІМІЯ Методичні вказівки ДЛЯ ПІДГОТОВКИ ДО ПРАКТИЧНИХ ЗАНЯТЬ З БІОЛОГІЧНОЇ ХІМІЇ (Для студентів медичних факультетів) Затверджено вченою радою ХНМУ. Протокол № 4 від 27.04.2017 р. Approved by the Scientific Council of KhNMU. Protocol 4 (April 27, 2017) Харків ХНМУ 2017 Self-study guide for students of general medicine faculty in biochemistry. Part 4. Functional biochemistry / comp. O. Nakonechna, S. Stetsenko, L. Popova, A. Tkachenko. – Kharkiv : KhNMU, 2017. – 80 p. Методичні вказівки для підготовки до практичних занять з біологічної хі- мії (для студентів медичних факультетів). Частина 4. Функціональна біохімія / упоряд. О.А. Наконечна, С.О. Стеценко, Л.Д. Попова, А.С. Ткаченко. – Харків : ХНМУ, 2017. – 80 с. Authors Nakonechna O. Stetsenko S. Popova L. Tkachenko A. Автори: О.А. Наконечна С.О. Стеценко Л.Д. Попова А.С. Ткаченко - 2 - SOURCES For preparing to practical classes in "Biological Chemistry" Basic Sources 1. Біологічна і біоорганічна хімія: у 2 кн.: підручник. Кн. 2. Біологічна хі- мія / Ю.І. Губський, І.В. Ніженковська, М.М. Корда, В.І. Жуков та ін.; за ред. Ю.І. Губського, І.В. Ніженковської. – К.: ВСВ «Медицина», 2016. – 544 с. 2. Губський Ю.І. Біологічна хімія. Підручник / Губський Ю.І. – Київ- Вінниця: Нова книга, 2007. – 656 с. 3. Губський Ю.І. Біологічна хімія / Губський Ю.І. – Київ–Тернопіль: Укрмедкнига, 2000. – 508 с. 4. Гонський Я.І. Біохімія людини. Підручник / Гонський Я.І., Максимчук Т.П., Калинський М.І. – Тернопіль: Укрмедкнига, 2002.
    [Show full text]
  • Structural and Functional Diversity of Microbial Globins
    European Journal of Molecular & Clinical Medicine ISSN 2515-8260 Volume 07, Issue 07, 2020 Structural And Functional Diversity Of Microbial Globins 1Shiv Kumar 1Department of Medical Laboratory Sciences (School of Physiotherapy and Paramedical Sciences), Lovely Professional University, Phagwara, Punjab (India) – 1444 Email ID: [email protected]; ABSTRACT Hemoglobin and myoglobin are heme proteins that can bind oxygen reversibly and were first reported in vertebrates. Later on, occurrence of hemoglobin was found in all forms of life ranging from prokaryotes to eukaryotes. Myxobacteria are Gram-negative, rod-shaped eubacteria and that belong to delta proteobacteria. They predominantly thrive in soil and have very large genome size with high G+C content in comparison to other eubacteria. It is evident that the globins have been characterized predominantly from bacteria involved in photosynthesis, nitrogen fixation andpathogenicity, where these are implicated in and the protection of photosynthetic machinery from the oxidative damage,protection of nitrogen fixing enzyme from nitrosative and oxidative stress and the virulence of the host, respectively. Keywords: Myxobacteria, hemoglobin, myoglobin, phytoglobin, androglobin. 1. INTRODUCTION Globins are heme containing proteins which comprise five to eight α-helices that are connected by short intervening loops and have a common characteristic of binding oxygen reversibly [1-4]. These are widely reported in all the three domains of life forms such as Archaebacteria, eubacteria and eukaryotes [1]. In addition to their well-known function of oxygenstorage and transport, they are also involved in nitric oxide detoxification, oxygensensing or act as oxidation-reduction sensors [2]. Globins containhighly conserved structural folds, which build the protein crevice to hold the heme group [5, 6].
    [Show full text]
  • Circulatory Systems Vertebrate Hearts Respiratory Pigments
    3/25/2015 Circulatory Systems Vertebrate hearts • Chambers isolate pulmonary and • Open vs. closed systemic circuits • Components of • Blood pressure and regulation of hemolymph or blood flow rates • Hearts • Vasoconstriction and dilation – Simplest forms are thickened smooth • Flow velocity minimized, area muscle in arteries maximized in capillaries • Flow pressure minimized in largest veins Respiratory Pigments • Molecules that bind oxygen, facilitate transfer from respiratory surface to tissues that need it. Tissues Lungs Bind Release High PO2 Low PO2 • Oxygen affinity – [ ] • % = x 100 [] 1 3/25/2015 Structure of Hemoglobin Respiratory Pigments Oxygen Molecular • Oxyhemoglobin – bound with O2, reversible Color Cells or Pigment Structure capacity Weight Animal Groups (change) Solution • Deoxyhemoglobin – not bound with oxygen, Fe reduced (ml g-1) (kDa) Mollusks, • Carbaminohemoglobin – bound with CO , reversible Hemocyanin Blue 2 Protein+Cu2+ 0.3-0.5 25-7000 Solution cephalopods, (colorless) • Carbon monoxide hemoglobin – combined with CO, not arthropods Nematodes, reversible Hemoglobin Protein+heme Red 1.2-1.4 16-2000 Either annelids, +Fe2+ (purple/blue) vertebrates Protein+heme Annelids, marine Chlorocruorin Green 0.6-0.9 3000 Solution +Fe2+ polychaetes Protein Violet Brachiopods, some Hemerythrin 1.6-1.8 16-125 Either +Fe2+ (colorless) marine annelids • Intracellular vs. solution • Various other forms, recall gene families Before/after methemoglobinemia P50 Oxygen carrying capacity • Total oxygen capacity of blood depends on
    [Show full text]
  • The Functioning of the Haemocyanin of the Terrestrial Christmas Island Red Crab Gecarcoidea Natalis and Roles for Organic Modulators
    The Journal of Experimental Biology 201, 3233–3244 (1998) 3233 Printed in Great Britain © The Company of Biologists Limited 1998 JEB1579 THE FUNCTIONING OF THE HAEMOCYANIN OF THE TERRESTRIAL CHRISTMAS ISLAND RED CRAB GECARCOIDEA NATALIS AND ROLES FOR ORGANIC MODULATORS AGNIESZKA M. ADAMCZEWSKA* AND STEPHEN MORRIS School of Biological Sciences (A08), University of Sydney, Sydney, NSW 2006, Australia *Present address: Oregon Institute of Marine Biology, University of Oregon, PO Box 5389, Charleston, OR 97420, USA (e-mail: [email protected]) Accepted 24 August; published on WWW 10 November 1998 Summary Gecarcoidea natalis is a land crab that migrates annually O2-affinity in G. natalis was unique among the crustaceans, several kilometres to breed. The O2-binding properties of because an increase in L-lactate concentration decreased haemocyanin in G. natalis were investigated in vitro to test the haemocyanin O2-affinity. The effect of L-lactate on the idea that the O2-binding properties of the haemocyanin haemocyanin O2-affinity (∆logP50/∆log[lactate]) was time- of land crabs are not dependent on circulating modulators dependent and decreased from a maximum of 0.044 on day and to provide a model of haemocyanin functioning during 1 to 0.001 after 4 days of storage at 4 °C. The presence of exercise. The affinity of the haemocyanin for O2 decreased an unknown dialysable and unstable factor in the with increasing temperature (change in the heat of haemolymph is postulated to explain the time-dependent −1 oxygenation; ∆H=−59 kJ mol ). The haemocyanin of G. effect of L-lactate on haemocyanin O2-binding properties.
    [Show full text]
  • The Haemoglobin Subunits Alpha and Beta: Old and New Genetic Variants in the Italian Mediterranean Buffalo
    Czech Journal of Animal Science, 64, 2019 (7): 279–290 Original Paper https://doi.org/10.17221/14/2018-CJAS The haemoglobin subunits alpha and beta: Old and new genetic variants in the Italian Mediterranean buffalo Rosario Rullo1, Aldo Di Luccia2, Elena Ciani3*, Elisa Pieragostini4 1Institute for the Animal Production Systems in the Mediterranean Environment, Napoli, Italy 2Department of Agricultural, Food and Environmental Sciences, University of Foggia, Foggia, Italy 3Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari “Aldo Moro”, Bari, Italy 4Department of Emergency and Organ Transplantation, University of Bari “Aldo Moro”, Bari, Italy *Corresponding autor: [email protected] Citation: Rullo R., Di Luccia A., Ciani E., Pieragostini E. (2019): The haemoglobin subunits alpha and beta: Old and new genetic variants in the Italian Mediterranean buffalo. Czech J. Anim. Sci., 64, 279–290. Abstract: Haemoglobin (HB), the most widely distributed respiratory pigment in the animal kingdom, is among the best characterized oxygen-binding proteins, both at functional and molecular level. However, very little informa- tion is available about the genomic features of HB in river buffalo (Bubalus bubalis), even though there are reports in literature confirming the presence of interesting polymorphisms at the protein level in Mediterranean buffalo. We hence address the characterization of exonic as well as intronic nucleotide polymorphism in the haemoglobin subunit alpha and beta in a set of nine Italian Mediterranean buffaloes exhibiting different HB phenotypes. The nine buffaloes were selected from a random set of 398 samples, previously analysed for their HB protein polymorphism, in order to account for both globin variants and the evolution of intron variability within the most common domes- ticated species of the family Bovidae.
    [Show full text]
  • Globins in the Marine Annelid Platynereis Dumerilii Shed New Light
    Globins in the marine Annelid Platynereis dumerilii shed new light on hemoglobin evolution in Bilaterians Solène Song, Viktor Starunov, Xavier Bailly, Christine Ruta, Pierre Kerner, Annemiek Cornelissen, Guillaume Balavoine To cite this version: Solène Song, Viktor Starunov, Xavier Bailly, Christine Ruta, Pierre Kerner, et al.. Globins in the marine Annelid Platynereis dumerilii shed new light on hemoglobin evolution in Bilaterians. 2020. hal-02410194v2 HAL Id: hal-02410194 https://hal.archives-ouvertes.fr/hal-02410194v2 Preprint submitted on 8 Dec 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution - NonCommercial - NoDerivatives| 4.0 International License Manuscript Click here to access/download;Manuscript;Song_et_al_2e_revision.docx Click here to view linked References Globins in the marine annelid Platynereis dumerilii shed new light on hemoglobin 1 2 evolution in bilaterians. 3 4 5 Solène Song 1, 2, Viktor Starunov 3, Xavier Bailly 4, Christine Ruta 5, Pierre Kerner 1, Annemiek 6 2 1 7 J.M. Cornelissen and Guillaume Balavoine * 8 9 10 1. Université de Paris, CNRS, Institut Jacques Monod, Paris, France 11 12 2. Université de Paris, CNRS, Laboratoire Matière et Systèmes Complexes, Paris, 13 France 14 15 3.
    [Show full text]
  • Placental (К^Сgeké S
    PDF hosted at the Radboud Repository of the Radboud University Nijmegen The following full text is a publisher's version. For additional information about this publication click this link. http://hdl.handle.net/2066/147916 Please be advised that this information was generated on 2021-09-24 and may be subject to change. PLACENTAL (К^СGEKÉ S * Уп^ггі«» ¿л i ι) Дстг R.H.W. LORIJN ^ FETAL OXYGEN CONSUMPTION AND PLACENTAL OXYGEN EXCHANGE PROMOTORES PROF. DR LD. LONGO PROF. DR Т.К.A.B. ESKES CO-REFERENT DR L.L.H. PEETERS FETAL OXYGEN CONSUMPTION AND PLACENTAL OXYGEN EXCHANGE PROEFSCHRIFT ter verkrijging van de graad van doctor in de geneeskunde aan de Katholieke Universiteit te Nijmegen, op gezag van de Rector Magnificus Prof. Dr. P.G.A.B. Wijdeveld, volgens besluit van het College van Decanen in het openbaar ter verdediging op vrijdag 9 mei 1980 des namiddags te 2.00 uur precies door RONALD HANS WILMAR LORIJN geboren te 's Gravenhage Krips Repro Meppel 1980 This study was performed during a two year research fellowship in the Department of Perinatal Biology, Loma Linda University, School of Medicine, Loma Linda, California 92350, U.S.A., under the guidance of Prof. Dr. L. D. Longo. A Nato Grant awarded by the Netherlands Organization for the Advancement of Pure Research (Z. W. O. ) and U. S. P. H. S. Grant 03807 furnished the financial support of the investigation. "Therefore, one concludes that one and the same soul governs the bodies and one and the same nourishes both. " Leonardo da Vinci Copyright 1980.
    [Show full text]
  • Nader G. Abraham & Attallah Kappas
    Home About Thomson Reuters Press Room Contact Us ● ScienceWatch Home ● Inside This Month... ● Interviews Featured Interviews Author Commentaries 2009 : July 2009 - New Hot Papers : Nader G. Abraham & Attallah Kappas Institutional Interviews Journal Interviews NEW HOT PAPERS - 2009 Podcasts July 2009 ● Analyses Nader G. Abraham & Attallah Kappas talk with ScienceWatch.com about this month's New Hot Featured Analyses Paper in the field of Pharmacology & Toxicology. What's Hot In... Article Title: Pharmacological and clinical aspects of heme Special Topics oxygenase Authors: Abraham, NG;Kappas, A Journal: PHARMACOL REV, Volume: 60, Issue: 1, Page: 79-127, Year: ● Data & Rankings MAR 2008 * New York Med Coll, Dept Med & Pharmacol, Basic Sci Bldg, Valhalla, NY 10595 USA. Sci-Bytes * New York Med Coll, Dept Med & Pharmacol, Valhalla, NY 10595 USA. Fast Breaking Papers * Rockefeller Univ Hosp, New York, NY 10021 USA. New Hot Papers Emerging Research Fronts Fast Moving Fronts The paper collates and brings up-to-date much of the current knowledge relevant to pharmacology and to clinical medicine concerning the enzyme heme oxygenase (HO), which catabolizes the breakdown of the Corporate Research Fronts oxygen-carrying respiratory pigment called heme. In this process, heme is converted to the bile pigment Research Front Maps bilirubin; carbon monoxide is generated, and the iron atom, which is complexed by the porphyrin ring of the Current Classics molecule, is released. Top Topics The background to the discovery of HO is important to appreciate. The Laboratory of Pharmacology, at Rising Stars The Rockefeller University Hospital, in which this work was done, was established in 1967 by Professor Attallah Kappas, who then headed the laboratory and also served subsequently as Physician-in-Chief of New Entrants The Rockefeller Hospital and Vice-President of the University.
    [Show full text]