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Human Plasma and Recombinant Hemopexins: Heme Binding Revisited
International Journal of Molecular Sciences Article Human Plasma and Recombinant Hemopexins: Heme Binding Revisited Elena Karnaukhova 1,*, Catherine Owczarek 2, Peter Schmidt 2, Dominik J. Schaer 3 and Paul W. Buehler 4,5,* 1 Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, USA 2 CSL Limited, Bio21 Institute, Parkville, Victoria 3010, Australia; [email protected] (C.O.); [email protected] (P.S.) 3 Division of Internal Medicine, University Hospital of Zurich, 8091 Zurich, Switzerland; [email protected] 4 Department of Pathology, The University of Maryland School of Medicine, Baltimore, MD 21201, USA 5 The Center for Blood Oxygen Transport and Hemostasis, Department of Pediatrics, The University of Maryland School of Medicine, Baltimore, MD 21201, USA * Correspondence: [email protected] (E.K.); [email protected] (P.W.B.) Abstract: Plasma hemopexin (HPX) is the key antioxidant protein of the endogenous clearance pathway that limits the deleterious effects of heme released from hemoglobin and myoglobin (the term “heme” is used in this article to denote both the ferrous and ferric forms). During intra-vascular hemolysis, heme partitioning to protein and lipid increases as the plasma concentration of HPX declines. Therefore, the development of HPX as a replacement therapy during high heme stress could be a relevant intervention for hemolytic disorders. A logical approach to enhance HPX yield involves recombinant production strategies from human cell lines. The present study focuses on a biophysical assessment of heme binding to recombinant human HPX (rhHPX) produced in the Expi293FTM (HEK293) cell system. -
MASSHEALTH TRANSMITTAL LETTER LAB-22 July 2002 TO
Commonwealth of Massachusetts Executive Office of Health and Human Services Division of Medical Assistance 600 Washington Street Boston, MA 02111 www.mass.gov/dma MASSHEALTH TRANSMITTAL LETTER LAB-22 July 2002 TO: Independent Clinical Laboratories Participating in MassHealth FROM: Wendy E. Warring, Commissioner RE: Independent Clinical Laboratory Manual (Laboratory HCPCS) The federal government has revised the HCFA Common Procedure Coding System (HCPCS) for MassHealth billing. This letter transmits changes for your provider manual that contain the new and revised codes. The revised Subchapter 6 is effective for dates of service on or after April 30, 2002. The codes introduced under the 2002 HCPCS code book are effective for dates of service on or after April 30, 2002. We will accept either the new or the old codes for dates of service through July 28, 2002. For dates of service on or after July 29, 2002, you must use the new codes to receive payment. If you wish to obtain a fee schedule, you may purchase Division of Health Care Finance and Policy regulations from either the Massachusetts State Bookstore or from the Division of Health Care Finance and Policy (see addresses and telephone numbers below). You must contact them first to find out the price of the publication. The Division of Health Care Finance and Policy also has the regulations available on disk. The regulation title for laboratory is 114.3 CMR 20.00: Laboratory. Massachusetts State Bookstore Division of Health Care Finance and Policy State House, Room 116 Two Boylston Street -
Clotting Phenomena at the Blood-Polymer Interface and Development of Blood Compatible Polymeric Surfaces
Clotting Phenomena at the Blood-Polymer Interface and Development of Blood Compatible Polymeric Surfaces Adriaan Bantjes In the past two decades many attempts have been made to relate surface and interfacial parameters with the blood compatibility of polymeric surfaces. It is however doubtful if by a single parameter the behaviour of blood on a surface can be predicted. Two major aspects of blood compatibility -- the prevention of platelet adhesion and the deactivation of the intrinsic coagulation system are determined by the measure and nature of competi- tive blood protein adsorption on the foreign surface. The adhesion of blood platelets is promoted by adsorbed fibrinogen and gamma globulin, while adsorbed albumin inhibits platelct adhesion. Heparinised surfaces do not adsorb fibrin and consequently no adhesion of platelets takes place. Othcr surfaces with low platelct adhesion are the hydrogels, certain block copolyetherurethanes, polyelectrolyte complexes and biolised proteins. Heparinised surfaces of the cationically bonded type inhibit the intrinsic coagulation as well, however this may be due to unstable coatings and heparin leakage. In the authors laboratory a synthetic heparinoid was prepared with the structure - [CH, - C(CH3) NHS03Na ~ C(H) COONa ~ CH2 --] with h, = (7.5 5 1 .O) x lo5 and an in vivo anticoagulant activity of 50% of heparin. Its coatings on PVC, using tridodecyltiietliyl-ammoniuni chloridc as a coupling agent, are stable in plasma and salt solutions and provide surfaces which show negligible platelet adhesion and a strong inhibition 01 the intrinsic coagulation on contact with blood. Similar results were found with polydimethylsiloxane surfaces coated with this heparinoid. 1. INTRODUCTION new blood compatible materials may be developed it is necessary to explain sotne of the mechanisms of blood co- The clinical use of blood contacting devices and prosthcses is agulation on intcraction with a foreign surface. -
The Effect of Gamma Globulin in Pustular Acne*
PRELIMINARY AND SHORT REPORT THE EFFECT OF GAMMA GLOBULIN IN PUSTULAR ACNE* LOREN W.SHAFFER,M.D., BENJAMIN SdHWIMMER, M.D. AND RENATO J.STANICCO,M.D. One of us (LWS) bad occasion to treat a young Clinical Response: Patient 1: New lesions ceased white man with gamma globulin for prophylaxisappearing immediately after the first injection. after exposure to infectious hepatitis. He wasBy the third week most of the cystic and pustular given two injections, 10 cc. each, of human Polio-lesions had dried up, and no new ones had ap- myelitis Immune Globulin, one week apart. Itpeared. Comedones were not decreased in number. was observed that shortly after the second injec-The patient maintained his improvement through tion, his severe pustular and indurated acnethe fifth week when the cystic and pustular lesions improved considerably. This observation led tobegan to recur. the present study, of which this is a preliminary Patient 2: New lesions continued to develop report. throughout the period of treatment and the one This study of the therapeutic effect of gammamonth follow up. globulin in pustular acne is coupled with a study Patient 3: There was no observable effect of of the serum protein and C-reactive protein levelstreatment. before and after treatment. Patient 4: The first improvement was seen in Method: Four patients in their late teens, other-the second week and by the third, all cystic and wise healthy, but with severe pustular and cysticpustular lesions were dry. The improvement acne that had been resistant to conventionallasted for two weeks after which the lesions methods of treatment were selected for the study.began to return. -
Syllabus: Page 23
The University of Texas at El Paso College of Health Sciences Clinical Laboratory Science Program CLSC 3364 Hematology II Course Outline Spring What do you see? What is in your Head? Video or audio recordings will not be permitted. Instructor M. Lorraine Torres, Ed. D, MT (ASCP) College of Health Sciences Room 423 Phone: 747-7282 E-Mail: [email protected] Office Hours TR 3:00 – 4:00 p.m., Friday 2 – 3 p.m. or by appointment Class Schedule Monday and Wednesday 11:00 – 12:30 A.M. HSCI 135 Course Description This course is a sequel to Hematology I. It will include but is not limited to the study of the white blood cells with emphasis on white cell formation and function and the etiology and treatment of white blood cell disorders. This course will also encompass an introduction to hemostasis and laboratory determination of hemostatic disorders. Prerequisite; CLSC 3356 & CLSC 3257. Topical Outline 1. Maturation series and biology of white blood cells 2. Disorders of neutrophils 3. Reactive lymphocytes and Infectious Mononucleosis 4. Acute and chronic leukemias 5. Myelodysplastic syndromes 6. Myeloproliferative disorders 7. Multiple Myeloma and related plasma cell disorders 8. Lymphomas 9. Lipid (lysosomal) storage diseased and histiosytosis 10. Hemostatic mechanisms, platelet biology 11. Coagulation pathways 12. Quantitative and qualitative vascular and platelet disorders (congenital and acquired) 13. Disorders of plasma clotting factors 14. Interaction of the fibrinolytic, coagulation and kinin systems 15. Laboratory methods REQUIRED TEXTBOOKS: same books used for Hematology I Keohane, E.M., Smith, L.J. and Walenga, J.M. 2016. Rodak’s Hematology: Clinical Principles and applications. -
Pathological Conditions Involving Extracellular Hemoglobin
Pathological Conditions Involving Extracellular Hemoglobin: Molecular Mechanisms, Clinical Significance, and Novel Therapeutic Opportunities for alpha(1)-Microglobulin Gram, Magnus; Allhorn, Maria; Bülow, Leif; Hansson, Stefan; Ley, David; Olsson, Martin L; Schmidtchen, Artur; Åkerström, Bo Published in: Antioxidants & Redox Signaling DOI: 10.1089/ars.2011.4282 2012 Link to publication Citation for published version (APA): Gram, M., Allhorn, M., Bülow, L., Hansson, S., Ley, D., Olsson, M. L., Schmidtchen, A., & Åkerström, B. (2012). Pathological Conditions Involving Extracellular Hemoglobin: Molecular Mechanisms, Clinical Significance, and Novel Therapeutic Opportunities for alpha(1)-Microglobulin. Antioxidants & Redox Signaling, 17(5), 813-846. https://doi.org/10.1089/ars.2011.4282 Total number of authors: 8 General rights Unless other specific re-use rights are stated the following general rights apply: Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights. • Users may download and print one copy of any publication from the public portal for the purpose of private study or research. • You may not further distribute the material or use it for any profit-making activity or commercial gain • You may freely distribute the URL identifying the publication in the public portal Read more about Creative commons licenses: https://creativecommons.org/licenses/ Take down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. -
Gamma Globulin”
CLINICAL APPLICATION OF A SIMPLE METHOD FOR ESTIMATING “GAMMA GLOBULIN” B. V. Jager, Margaret Nickerson J Clin Invest. 1948;27(2):231-238. https://doi.org/10.1172/JCI101938. Research Article Find the latest version: https://jci.me/101938/pdf CLINICAL APPLICATION OF A SIMPLE METHOD FOR ESTIMATING "GAMMA GLOBULIN" 1 By B. V. JAGER AND MARGARET NICKERSON (From the Department of Medicine, School of Medicine, University of Utah, Salt Lake City) (Received for publication August 11, 1947) The electrophoretic technique offers the most cipitate is finely emulsified in 3.0 ml. of 33.3 per cent accurate method for serum fractionation. This saturated ammonium sulfate. The tube is recentrifuged for 30 minutes and the supernatant fluid is discarded. permits a quantitative separation of serum into The precipitate is dissolved in 10 ml. of saline and an albumin and into three major globulin fractions aliquot is employed to determine its protein content, using which are designated as alpha, beta and gamma a biuret method such as that of Weichselbaum (2). components. In recent years electrophoretic anal- Triplicate determinations may be made with an *yses of serum proteins have been performed by accuracy of + 2 per cent. Electrophoretic studies many investigators in a variety of diseases. The indicate that 73 to 83 per cent of this protein accumulated data from these studies have now at- fraction consists of gamma globulin, the remainder tained sufficient size and agreement that they may consisting of alpha and beta globulins. From 70 to be of value as an aid in the differential diagnosis 82 per cent of the total gamma globulin present of certain diseases or for following the course of in the serum is recovered in this fraction. -
Study of Plasma Glycoglobulin Hemochromogens
Proceedings of the National Academy of Sciences Vol. 68, No. 3, pp. 609-613, March 1971 Heme Binding and Transport-A Spectrophotometric Study of Plasma Glycoglobulin Hemochromogens DAVID L. DRABKIN Department of Biochemistry, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pa. 19104 Communicated by Britton Chance, December 16, 1970 ABSTRACT A hitherto unreported phenomenon is the content was only 0.004-0.007 mmol/liter (or 0.04-0.07% of immediate production of the spectrum of ferrohemo- the hemoglobin content of whole blood). At this concentration chromogens (in the presence of sodium dithionite) upon the addition in vitro of hydroxyhemin (pH 7.6-7.8) to the all of the hemoglobin present was probably in the form of plasmas or sera, as well as to certain Cohn plasma protein hemoglobin-haptoglobin (11). In most cases the serum was fractions, of all mammalian species thus far examined. used directly; in some it was found desirable to dilute the This distinctive reaction is characteristic of a coordination serum 1:1 with 0.2 M phosphate buffer, pH 7.6, prior to the complex with heme iron, and is ascribed to a remarkable affinity for heme of certain plasma glycoglobulins, which addition of heme and reductant. Plasma protein fractions IV-1, include hemopexin. Spectrophotometry has permitted IV4, IV-7, and VI of most of the above species [prepared by estimations of the specific heme-binding capacity (as the alcohol-low temperature technique (12-15) and obtained ferrohemochromogen) of the plasmas, the rate of removal mainly from the Nutritional Biochemical Corp. ] were also ex- from plasma of injected heme, and the production of bile amined. -
Modeling to Understand Plant Protein Structure-Function Relationships—Implications for Seed Storage Proteins
molecules Review Modeling to Understand Plant Protein Structure-Function Relationships—Implications for Seed Storage Proteins 1,2, 1, 2 1, Faiza Rasheed y, Joel Markgren y , Mikael Hedenqvist and Eva Johansson * 1 Department of Plant Breeding, The Swedish University of Agricultural Sciences, Box 101, SE-230 53 Alnarp, Sweden; [email protected] (F.R.); [email protected] (J.M.) 2 School of Chemical Science and Engineering, Fibre and Polymer Technology, KTH Royal Institute of Technology, SE–100 44 Stockholm, Sweden; [email protected] * Correspondence: [email protected] These authors contributed equally to this work. y Received: 2 January 2020; Accepted: 14 February 2020; Published: 17 February 2020 Abstract: Proteins are among the most important molecules on Earth. Their structure and aggregation behavior are key to their functionality in living organisms and in protein-rich products. Innovations, such as increased computer size and power, together with novel simulation tools have improved our understanding of protein structure-function relationships. This review focuses on various proteins present in plants and modeling tools that can be applied to better understand protein structures and their relationship to functionality, with particular emphasis on plant storage proteins. Modeling of plant proteins is increasing, but less than 9% of deposits in the Research Collaboratory for Structural Bioinformatics Protein Data Bank come from plant proteins. Although, similar tools are applied as in other proteins, modeling of plant proteins is lagging behind and innovative methods are rarely used. Molecular dynamics and molecular docking are commonly used to evaluate differences in forms or mutants, and the impact on functionality. -
Methemalbumin. Ii. Effect of Pamaquine and Quinine on Pathways of Hemoglobin Metabolism
METHEMALBUMIN. II. EFFECT OF PAMAQUINE AND QUININE ON PATHWAYS OF HEMOGLOBIN METABOLISM William D. Blake J Clin Invest. 1948;27(3):144-150. https://doi.org/10.1172/JCI101954. Research Article Find the latest version: https://jci.me/101954/pdf METHEMALBUMIN. II. EFFECT OF PAMAQUINE AND QUININE ON PATHWAYS OF HEMOGLOBIN METABOLISM 1, 2 By WILLIAM D. BLAKE 8 (From the Department of Medicine, New York University College of Medicine, and the Research Service, Third [New York University] Medical Division, Goldwater Memorial Hospital, New York City) (Received for publication March 12, 1947) INTRODUCTION laria during the study but the period immediately fol- lowing malaria was avoided because of the questionable Methemalbuminemia has been described in as- status of certain functions of the liver (10, 11, 12). sociation with massive intravascular hemolysis Serunm bilirubin and bromsulfalein retention tests were (1, 2, 3, 4) or with limited hemolysis in the pres- normal, unless specifically mentioned. ence of liver disease (1, 5). Similarly, the in- Pamaquine naphthoate and quinine sulfate were admin- istered orally, the dosage in each case being expressed jection of large amounts of hemoglobin may result in terms of the free base. Plasma pamaquine (13) and in methemalbuminemia (1), whereas smaller quinine concentrations (14) were estimated at intervals amounts do so only in the presence of a damaged to ascertain reliability of drug intake. Pamaquine dosage liver (6). Hematin injected intravenously rapidly regimens were either 15 mg. every four hours or 10 mg. combines with serum albumin to form methemal- every eight hours. Quinine was given as the sulfate in 0.6 gram doses every eight hours. -
Dietary and Lifestyle Factors Modulate the Activity of the Endogenous
antioxidants Article Dietary and Lifestyle Factors Modulate the Activity of the Endogenous Antioxidant System in Patients with Age-Related Macular Degeneration: Correlations with Disease Severity Zofia Ula ´nczyk 1 , Aleksandra Grabowicz 2, El˙zbietaCecerska-Hery´c 3, Daria Sleboda-Taront´ 3, El˙zbietaKrytkowska 2, Katarzyna Mozolewska-Piotrowska 2, Krzysztof Safranow 4 , Miłosz Piotr Kawa 1, Barbara Doł˛egowska 3 and Anna Machali ´nska 2,* 1 Department of General Pathology, Pomeranian Medical University, 70-111 Szczecin, Poland; zofi[email protected] (Z.U.); [email protected] (M.P.K.) 2 First Department of Ophthalmology, Pomeranian Medical University, 70-111 Szczecin, Poland; [email protected] (A.G.); [email protected] (E.K.); [email protected] (K.M.-P.) 3 Department of Laboratory Medicine, Pomeranian Medical University, 70-111 Szczecin, Poland; [email protected] (E.C.-H.); [email protected] (D.S.-T.);´ [email protected] (B.D.) 4 Department of Biochemistry and Medical Chemistry, Pomeranian Medical University, 70-111 Szczecin, Poland; [email protected] * Correspondence: [email protected] Received: 17 August 2020; Accepted: 2 October 2020; Published: 5 October 2020 Abstract: Age-related macular degeneration (AMD) is a common cause of blindness in the elderly population, but the pathogenesis of this disease remains largely unknown. Since oxidative stress is suggested to play a major role in AMD, we aimed to assess the activity levels of components of the antioxidant system in patients with AMD. We also investigated whether lifestyle and dietary factors modulate the activity of these endogenous antioxidants and clinical parameters of disease severity. -
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