Everand Logo

Welcome to Everand!

  • Discover millions of ebooks, audiobooks, and so much more with a free trial

    Only $11.99/month after trial. Cancel anytime.

    Oxygen Transport in Red Blood Cells: Proceedings of the 12th Aharon Katzir Katchalsky Conference, Tours, France, 4–7 April 1984
    Oxygen Transport in Red Blood Cells: Proceedings of the 12th Aharon Katzir Katchalsky Conference, Tours, France, 4–7 April 1984
    Oxygen Transport in Red Blood Cells: Proceedings of the 12th Aharon Katzir Katchalsky Conference, Tours, France, 4–7 April 1984
    Ebook389 pages3 hours

    Oxygen Transport in Red Blood Cells: Proceedings of the 12th Aharon Katzir Katchalsky Conference, Tours, France, 4–7 April 1984

    ()

    Read preview

    About this ebook

    Oxygen Transport in Red Blood Cells contains the proceedings of the 12th Aharon Katzir Katchalsky Conference held at Tours, France on April 4-7, 1984. Organized into 16 chapters, this book begins with a discussion on the influence of heme pocket geometry on ligand binding to heme proteins. Subsequent chapters describe a genetic approach to producing oxygen affinity differences; clinical importance of the oxygen transport function of preserved red blood cells; methods for the measurement of oxygen equilibrium curves of red cell suspensions and hemoglobin solutions; and aspects of oxygen supply to tissue. Other chapters elucidate interactions between hemoglobin and erythrocyte membrane and membrane protein oxidation; incorporation of allosteric effectors of hemoglobin in red blood cells; and significance of low hemoglobin oxygen affinity.The interaction of ligands and other molecules with hemoglobin and the storage of red blood cells having incorporated exogenous allosteric effectors of hemoglobin are also explained.
    LanguageEnglish
    PublisherElsevier Science
    Release dateOct 22, 2013
    ISBN9781483160443
    Oxygen Transport in Red Blood Cells: Proceedings of the 12th Aharon Katzir Katchalsky Conference, Tours, France, 4–7 April 1984

    Related to Oxygen Transport in Red Blood Cells

    Related ebooks

    Medical For You

    View More
    View More

    Related podcast episodes

    Related articles

    • Article

      With the Nobel Prizes Around the Corner, It’s Crystal Ball Time

      Sep 25, 2017

      The scientists who pioneered immunotherapy and other cancer advances are among the favorites for this year's Nobel Prizes, which will be announced the first week of October.

      4 min read

    • Article

      What Defines a Stem Cell?

      Dec 27, 2018

      For the past three years, researchers at the Hubrecht Institute in the Netherlands have been painstakingly cataloging and mapping all the proliferating cells found in mouse hearts, looking for cardiac stem cells. The elusive cells should theoreticall

      5 min read

    • Article

      Comment Afingeronthepulse

      Jun 4, 2023

      Ifwe had a dollar for everyone who has written in to tell us about their amazing new “quantum device,” we could retire tomorrow. Everywhere you look, there are products claiming to heal you via newly tapped-into “frequencies” or “standing waves” or e

      3 min read

    • Article

      Discovery Of Unknown Lung Cell Points To New Target For Cystic Fibrosis Medicines

      Aug 1, 2018

      The discovery could shift the understanding of the basic biology of cystic fibrosis, provide potential new targets for therapies, and one day shake up the market for CF medications.

      4 min read

    • Article

      Bubbling Up

      Mar 22, 2020

      Bubbling Up
      9 min read

    • Article

      There’s An Urgent Need For New Carbon Monoxide Poisoning Treatments. Could Bright Light Be An Antidote?

      Oct 9, 2019

      Experts say there's an urgent need for new treatments for carbon monoxide poisoning. One idea? Combining bright lights and an artificial lung to clean the blood of the toxin.

      3 min read

    • Article

      Science And Environment

      Mar 4, 2022

      Climate breakdown is accelerating rapidly, many of the impacts will be more severe than predicted and there is only a narrow chance left of avoiding its worst ravages, the Intergovernmental Panel on Climate Change (IPCC) has said. Even at current lev

      2 min read

    • Article

      Scientists Map Path Into Cell’s Nucleus

      Apr 6, 2018

      Researchers have delineated the architecture of the nuclear pore complex in yeast cells. The biological blueprint they uncovered shares principles sometimes seen on a much larger scale in concrete, steel, and wire. “It reminds us of a suspension brid

      3 min read

    • Article

      A Luminous Journey Into Cellular Biology

      Sep 1, 2022

      The Song of the Cell: An Exploration of Medicine and the New Human Written By: Siddhartha Mukherjee Publisher: Penguin Allen Lane ISBN-13: 978-1847925985 Mukherjee, a physician, professor of medicine, and Pulitzer Prize–winning author (The Emperor of

      2 min read

    • Article

      Glowing Protein Reveals How Oxygen Moves Through Brains

      Apr 1, 2024

      A new bioluminescence imaging technique has created highly detailed, and visually striking, images of the movement of oxygen in the brains of mice. The human brain consumes vast amounts of energy, which is almost exclusively generated from a form of

      3 min read

    • Article

      Three U.S. Scientists Win Nobel Prize for Uncovering Inner Workings of the Biological Clock

      Oct 2, 2017

      The 2017 Nobel Prize in physiology or medicine was awarded to Jeffrey Hall, Michael Roshbash, and Michael Young for their discoveries of circadian rhythms.

      2 min read

    • Article

      Future Medical Tests Could Use Bits Of RNA

      Jun 13, 2018

      Scientists have devised an improved method for isolating and identifying tiny fragments of RNA in human blood products. The achievement could lead to powerful new ways to diagnose and track a wide range of medical conditions, say the researchers. On

      3 min read

    • Article

      Science And Environment

      Oct 7, 2022

      Humans produce a different odour when under pressure – and dogs can sniff it out, according to a Queen’s University Belfast study. Previous research suggested canines might pick up on human emotions, possibly through smell, but questions remained ove

      2 min read

    • Article

      Step by Step

      Jul 28, 2023

      Step by Step
      2 min read

    • Article

      Could ‘Reprogramming’ These Cells Fix Damaged Hearts?

      Feb 15, 2018

      Scientists hope to one day create new healthy heart muscle cells within a patient’s own ailing heart. A new study reveals key molecular details that should be useful in developing this ambitious approach. In the study, published in Cell Reports, rese

      2 min read

    • Article

      Who Wants To Live Forever?

      Mar 18, 2021

      Who Wants To Live Forever?
      2 min read

    • Article

      ‘Lung On A Chip’ Mimics Deadly Disease

      May 29, 2018

      New biotechnology could speed up the development of medicines to treat pulmonary fibrosis, one of the most common and serious forms of lung disease, research shows. Developing new medicines isn’t easy, researchers say, because it’s difficult to simul

      2 min read

    Related categories

    Reviews for Oxygen Transport in Red Blood Cells

    0 ratings

    0 ratings0 reviews

    What did you think?

    Tap to rate

    Review must be at least 10 words

      Book preview

      Oxygen Transport in Red Blood Cells - Claude Nicolau

      Israel

      Influence of Heme Pocket Geometry on Ligand Binding to Heme Proteins

      K.H. Winterhalter and E.E. Di Iorio,     Laboratorium fuer Biochemie I, Eidgenoessische Technische, Hochschule, ETH-Zentrum, Universitaetsstrasse 16, 8092 Zurich, Switzerland

      Publisher Summary

      This chapter discusses the influence of heme pocket geometry on ligand binding to heme proteins. For the binding to the heme-iron of a ligand molecule, three steps characterized by energy barriers are distinguished: (1) penetration of the ligand from the solvent, across the structured hydration shell, into the protein matrix; (2) diffusion through the matrix into the heme pocket; and (3) the binding to iron from inside the pocket. The geometry of the heme pocket is influenced by two main factors. The most prominent one is genetic variety of the protein. For a given heme protein, the geometry is influenced by fluctuations of the proteic structure and steric changes in the prostetic group and are caused by alterations of the position of the iron relative to the heme plane. This is often caused by structural changes in the protein and frequently entails changes of the position of the heme within the pocket.

      Oxygen binding, and its delivery to the place of consumption, is the continent in which the city of oxygen transport by red blood cells lies. The problem of oxygen transport is old, but new insight is gained every year. Table I gives an overview of the continent and the roads to and from the city. The levels of traffic regulation, as they are conceived presently, are also given.

      Table I

      The levels of regulation of O2 supply to tissues

      Oxygen, at its various places of consumption, is needed for a variety of different types of metabolism. They are summarized in table II. From this table it is evident that oxygen affects all walks of biochemistry in areobic organisms, from energy production to cancer.

      Table II

      Types of metabolisms in which oxygen is paramount

      As many of the regulatory mechanisms of oxygen transport by red blood cells (Table I.B) will be discussed by other participants of this conference, the topic of this talk is limited to the innermost events inside the hemoglobin molecule.

      The overall anatomy of a sperm whale myoglobin (SW-Mb) molecule (also representative of a hemoglobin chain) is given in fig. 1. For the binding to the heme-iron of a ligand molecule, coming from the solvent, at least three steps, characterized by energy barriers (Austin et. al., 1975), must be distinguished:

      Figure 1 Cross section of a sperm whale myoglobin molecule

      1. Penetration of the ligand from the solvent, across the structured hydration shell, into the protein matrix.

      2. Diffusion through the matrix into the heme pocket.

      3. Binding to iron from inside the pocket.

      The corresponding reaction scheme is summarized in fig. 2. Some detailed informations on steps 1 and 2, taken together, have recently been obtained (Jameson, et al., 1984). Studying the quenching of fluorescence of the porphyrin by oxygen in SW-Mb and normal adult human hemoglobin (Hb-A) lacking the iron atom in their heme, the authors have been able to distinguish between the velocities of oxygen aquisition by the protein (k+), of exit of the ligand form the protein (k−) and of its migration through the proteic matrix (X). These velocities are different for SW-Mb and Hb-A as shown in table III.

      Table III

      Kinetic parameters affecting the motion of oxygen in SW-Mb and Hb-A. See the text for the definitions of the rate constants.

      Figure 2 General reaction scheme between ligand and heme protein

      P denotes Protein; X denotes Ligand; subscript s denotes penetration from the solvent into the matrix, and viceversa; subscript m denotes diffusion through the matrix into the heme pocket, and viceversa; subscript h denotes binding to the heme from inside the pocket, and viceversa.

      On step 3 many more data have been accumulated in both monomeric heme proteins and model heme compounds, such as picket fence porphyrins (Collman, et al., 1983.a, 1983.b), pocket porphyrins (Hashimoto, et al., 1982) and chelated protoheme (Traylor, 1981).

      The geometry of the heme pocket is influenced by two main factors. The most prominent one is, of course, genetic variety of the protein. For a given heme protein, the geometry is influenced by fluctuations of the proteic structure and steric changes in the prostetic group, as they are caused by alterations of the position of the iron relative to the heme plane. This, in turn, is often caused by structural changes in the protein and frequently entails changes of the position of the heme within the pocket.

      Here we would like to report on the functional properties of some natural monomeric heme proteins. This might seem a disappointment to the present audience, as human hemoglobin is tetrameric. However, the relative functional propreties of the geometrically slightly different heme pockets in alpha and beta chains, contained in tetrameric proteins (Shaanan, 1983), vary differentially as allosteric changes take place. This is well exemplified by the binding of allosteric effectors. For instance 2, 3-DPG binds between the two beta chains, thus stabilyzing the low affinity conformation of Hb-A. The effect of this lowering of oxygen affinity is quantitatively more pronounced on alpha chains than on beta (Mansouri, and Winterhalter, 1974). The difference between alpha and beta chains in oxygen affinity in the high affinty state of hemoglobin is about 1.6 to 1.8 (Olson and Gibson, 1971, Sawicki and Gibson, 1977), but considerably higher in the low affinty state hemoglobin (Mansouri and Winterhalter, 1973, 1974). For clarity we will limit our considerations presently to monomeric heme proteins which have important differences in their heme pockets.

      The proteins investigated in this framework are: SW-Mb, normal human alpha and beta chains (alpha-A and beta-A), beta chains from hemoglobin Zurich (beta-ZH, beta63 E7 Arg) and liver fluke (Dicrocoelium dendriticum) hemoglobin (Dd-Hb), a monomeric hemoglobin which, among other structural modifications, has a glycine instead of the distal histidine (Wilson K.J., personal communication; Smit and Winterhalter, 1981). In table IV the kinetic and the calculated equilibrium constants for the binding of CO and oxygen to different heme proteins are reported. Even a superficial look at the listed rates shows how broad their range of variability is. A change of around three orders of magnitude, for both the CO association and dissociation velocities, is observed. In contrast, smaller variations are found for oxygen. It should be born in mind that all these proteins have the same overall tertiary structure, the same heme, inserted in a hydrophobic pocket, as the active site and a histidine as the proximal ligand of the

      Enjoying the preview?
      Page 1 of 1