DOCSLIB.ORG

Sourcebook in Forensic Serology, Immunology, and Biochemistry

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Sourcebook in Forensic Serology, Immunology, and Biochemistry UNIT VII. HEMOGLOBIN, SERUM GROUP SYSTEMS, HLA AND OTHER GENETIC MARKERS Hemoglobin SECTION 38. HEMOGLOBIN 38.1 Introduction Hemoglobin (Hb)is the major protein of human red cells, forth. Hemoglobins exist which contain only one kind of comprising about 95% of their dry weight. Adult human chain: Hb H is B4, for example, and Hb Bart's is 7,. blood normally contains from about 4 million to 6.5 million Jones (1961) pointed out that hemoglobin structural red cells per mm3 blood, the average figure being slightly heterogeneity can be classified as follows: (1) Maturation higher for men. Hemoglobin itself is present in concentra- heterogeneity, which refers to the fact that different tions of about 14 to 16 g per 100 mP blood. It is the oxygen hemoglobins are normally synthesized during different transporting protein in higher animals; without a molecule stages of development. There are embryonic, fetal and adult having its properties, complex multicellular aerobic life as hemoglobins. (2) Minor hemoglobin heterogeneity, which we know it would not be possible. refers to the presence of small amounts of structurally dif- Hemoglobin is one of the most extensively studied of all ferent but normal hemoglobins along with the major proteins, and its literature fills many volumes. As noted in component characteristic of a particular stage of develop- section 5.1, it acquired its present name over 100 years ago ment; and (3) genetic heterogeneity, which refers to the (Hoppe-Seyler, 1864). In forensic serology, hemoglobiin is various "abnormal" hemoglobin variants. Many of these important in two principal contexts: (1) Blood is normally are thought to be the result of point mutations, and with a idenad in questioned samples by procedures designed to few exceptions, variant hemoglobins are very rare. The ex- demonstrate the presence of hemoglobin; and (2) hemo- cellent review of hemoglobins by Huisrnan (1%9) was globin exhibits a very large number of genetic variants, a organized according to this clasiication of heterogeneity. few of which are comparatively common and conveniently 38.2.1 Normal adult hemoglobins detectable by electrophoretic and/or isoelectrofocusing procedures. Many of the reactions of hemoglobin, which The structural studies on normal adult hemoglobins were form the basis of blood identification techniques, depend prompted in part by the recognition that the sickle cell con- upon the heme moiety of the molecule. These were discussed dition represented a diWete mol~~ularalteration in the in detail in unit 11, sections 4 through 7. Hemoglobin Hb molecule. Structural studies on nonnal adult and fetal, v-~s, which can serve as genetic markers, are discussed and variant hemoglobins were carried out simultaneously in in this section. ~bF, which discussed in section 8.3.1 as an effort to relate the detailed structures to the genetics. a marker for the bl&d of fetuses and young children, is also Most of these studies occurred in conjunction with the discussed here. Studies on hemoglobin variants and their development of presentday understandings of biochemical detailed structures have contributed sisnificantly to our cur- genetics (section 1.2.2), and have contributed importantly to rent understanding of molecular genetics. them. The major normal adult hemoglobin is called Hb A. It 38.2 Hemoglobin Structure has been called Hb A,, Ao and AII at different times (Holm- The structure of hemoglobin can be described at several quist and Schroeder, 1%6a), but these latter usages are now different levels. First, the molecule is a subunit protein, and discouraged (see in section 38.2.3.6). Hb A is a tetramer may be described in terms of the polypeptide chains that composed of two a and two /3 chains, and its structure is writ- make it up. Second, the detailed structure of each type of ten a2B2.Each polypeptide chain is associated with a heme subunit polypeptide chain can be described in terms of group (Figures 4.4 and 4.5). Intact Hb A thus has 4 heme amino acid sequence, and in terms of helical and nonhelical groups, and its MW is 64,450. The complete amino acid se- regions. Finally, the x-ray data have made possible a de- quences of the a and 6 chains were worked out in the early tailed description of the three-dimensional structure for 1%0's, and are shown in Figure 38.1 (Braunitzer et al., some of the hemoglobins. Detailed structures will be dis- 1%1; Konigsberg et al., 1%1). The sequencing studies have cussed briefly in the sections below. been well reviewed by Braunitzer et al. (1964). Part of the The hemoglobiin molecule is tetrameric, consisting of four stability of protein molecules arises from the a-helical associated polypeptide chains held together by noncovalent arrangement of the polypeptide chains (section 1.1.2.1). forces. One heme group is associated with each polypeptide This structw feature was predicted by Pauling and Corey, chain. Most hemoglobins consist of two a chains and two and has since been found to occur widely in nature (Pauling, none chains. The non-cr chainscan be 8, y, 6, e or J= Normal 1W). The helical structure of the polypeptide chains of Hb adult hemoglobm is designated Hb A, and consists of two a has been worked out using x-ray crystallographic and other aud two /3 chains. Its structure may thus be written: ~~282. techniques. The polypeptide chains consist of a series of Sily,Hb A2,a minor adult hemoglobin, has the struc- helical regions which are periodically interrupted. These tun ~26,.Normal fetal hemoglobin, Hb F, is azyl, and so helical regions are indicated by upper case letters, as shown Sourcebook in Forensic Serology, Immunologv, and Biochemistry I Pha 40 (6 Pro - Thr - Thr . LI. - Thr .Tvr - Phe .Pm - Hi. - Phe - Asp - Lmu -S.r C - CO ICE1 m 66 80 55 Gly ,Ala -Val -Ah - Awn .Thr .L.u .AIa - Asp - Ah .Val - Lvr .Lvs - Glv -%- Gly - Lys -Val - Gln - AIa - Sn / "M /nh ' 0. I 80 90 AIa - Leu .Sar - AL. .Lau - Sm - Hh- L*. .LWU- Arp \ IFFG Val I 110 106 100 95 Asp Leu - Hb - Ah -Ah - Lou - Tkr .Val - Lou - Leu - Cvs - His - Sar .Leu .Lw - Lva .Phe - Ann -Val - Pro 115 A$ on Glu 120 126 130 135 140 - me- Tkr .Pm .Ah -Val - Hls .All. Ser - Leu - Asp - Lys - Phs - Leu - AID - Sar -Val - Sar .Thr - Val - Leu. Thr - Sar .I.*. - Tvr - Arp n HC 6 10 15 Val - His .Leu - Thr - Pm - Glu - Glu - Lvs - Sar - Ala - Val - Thr - Ala - Lau - Tq- Gly - Lvs - Val NA L 6. cnnw 25 36 Tvr 40 45 W 55 Pm -Try - Thr - Gln - Arg - Phe - Phe - Glu - S.r - Phs - Gly - Asp - Leu .Ser .Thr .Pro .Asp .AIa . Val - Met C- CB 0 -1 GlY 75 70 65 60 Asn ,Hh Ah bu Glv Asp S.r .Phe Ah Gly Lau Val Lvs Lvr Gly Ah Lvs Val Lvs Pro - - - - - . - . - - [email protected] - . - - I L*U 0, AS; 1 80 Am EF I Leu \ T*. \ Gq 15 90 % Thr- Phe - Ah .Thr - Lwu - Ser - Glu - Leu .%-Cys - Asp - Lvs 7 -F Leu I FG 115 110 106 100 ni. GI* .Phe .His . Hi. .Ah - L.u .Val. Cv8 - Val - Leu - Val - Asn .Glv - Leu - Lmu - Arr - Phe - Asn - Glu .Pro - Asp -Val ./ I 120 LVS I ..- I GH Glu 125 130 135 110 145 \ ph. .mr.pro . pro .Val - Gln .Ah - Ah - Tyr - Gln - Lvs - Val .Val .Ala - Gly - Val - Ah - Asn - Ala - Leu - Ala - His .Lys .Tyr - His ' I nc Figure 38.1 a and 6 Chain Sequences in Hemoglobin. Helical regions are denoted by capital letters. The a 50 - 51 residues are denoted D6 - D7, Dl - D2. and CD8 - CD9 by different authors. There are no non-helical sequences BC and DE in a ; since there is no helical sequence D, CD is followed by E. There are no nonhelical sequences AB, BC and DE in 6. The proximal and distal histidines, which interact with heme, are boxed. Hemoglobin in Figure 38.1. The location of a particular amino acid genetically distinct from Hb A. In 1%1, Ingram and Strat- residue in the chain may thus be indicated in two ways: fust, ton discovered that Hb k2is not made up of the same poly- all the amino acid residues are numbered sequentially from peptide chains as Hb A, consisting instead of or chains and 6 the N-terminal end of the chain (as is the usual convention); chains. Hb A2has the subunit formula ~~262.The sequence of and second, the position of the amino acid in a particular the 6 chain has been determined, and is shown in Figure helical region (numbering from N-terminal to C-terminal) 38.2. Hb A2 represents about 2% of hemoglobins as a rule, may also be given. Transitional regions, which lie between but this proportion can be altered by pathological condi- two helical regions, are designated using two letters, the one tions. The other "minor" hemoglobins are not as well char- representing the immediately preceding (N-terminal side) acterized in general, but are thought to result from post- helical region, and the one representing the immediately synthetic alterations of the polypeptide chains, rather than following (C-terminal side) one. The N-terminal amino from distinct genetic loci. Hb AI,, for example, appears to acids which precede the first (A) helical region are denoted have hexose (probably glucose) condensed with the "NA", while the C-tennind amino acids which follow the N-terminal amino acid of the @chain (Holmquist and last (ZF) helical region are denoted "HC". A few examples Schroeder, 1%4, 1% and 1966b; Lehman and Huntsman, of this nomenclature (see in Figure 38.1): (1) the N-terminal 1974).
Load more

Recommended publications
  • Alexander's Seventh Phalanx Battalion Milns, R D Greek, Roman and Byzantine Studies; Summer 1966; 7, 2; Proquest Pg
    Alexander's Seventh Phalanx Battalion Milns, R D Greek, Roman and Byzantine Studies; Summer 1966; 7, 2; ProQuest pg. 159 Alexander's Seventh Phalanx Battalion R. D. Milns SOME TIME between the battle of Gaugamela and the battle of A the Hydaspes the number of battalions in the Macedonian phalanx was raised from six to seven.1 This much is clear; what is not certain is when the new formation came into being. Berve2 believes that the introduction took place at Susa in 331 B.C. He bases his belief on two facts: (a) the arrival of 6,000 Macedonian infantry and 500 Macedonian cavalry under Amyntas, son of Andromenes, when the King was either near or at Susa;3 (b) the appearance of Philotas (not the son of Parmenion) as a battalion leader shortly afterwards at the Persian Gates.4 Tarn, in his discussion of the phalanx,5 believes that the seventh battalion was not created until 328/7, when Alexander was at Bactra, the new battalion being that of Cleitus "the White".6 Berve is re­ jected on the grounds: (a) that Arrian (3.16.11) says that Amyntas' reinforcements were "inserted into the existing (six) battalions KC1:TCt. e8vr(; (b) that Philotas has in fact taken over the command of Perdiccas' battalion, Perdiccas having been "promoted to the Staff ... doubtless after the battle" (i.e. Gaugamela).7 The seventh battalion was formed, he believes, from reinforcements from Macedonia who reached Alexander at Nautaca.8 Now all of Tarn's arguments are open to objection; and I shall treat them in the order they are presented above.
    [Show full text]
  • Fetal and Embryonic Haemoglobins P
    Review Article J Med Genet: first published as 10.1136/jmg.10.1.50 on 1 March 1973. Downloaded from Journal of Medical Genetics (1973). 10, 50. Fetal and Embryonic Haemoglobins P. A. LORKIN MRC Abnormal Haemoglobin Unit, University Department of Biochemistry, Cambridge Haemoglobin has been the subject of intensive form a nearly spherical molecule with extensive research for many years and is one of the most areas of contact between unlike chains; the two thoroughly understood of all protein molecules. main types of contact are denoted alp, and alg2 The amino-acid sequences of haemoglobins from The tetramer exhibits cooperative behaviour or many species of animals have been determined haem-haem interaction. As each haem combines (tabulated by Dayhoff, 1969) and the molecular with oxygen the affinity of successive haems in- structures of horse and human haemoglobins have creases. The oxygen affinity curve of the tetramer been determined in great detail by x-ray crystallo- is sigmoidal and may be represented approximately graphy (Perutz et al, 1968a and b; Perutz 1969). A by the Hill equation:* mechanism of action of haemoglobin has been pro- = kpo2n posed (Perutz, 1970a and b and 1972). The y haemoglobins of higher organisms share a common +kpo2n tetrameric structure built up of two pairs of unlike Oxygen affinity data are usually presented in copyright. chains; the a chains containing 141 amino-acid terms of P102, the partial pressure of oxygen re- residues and the non-a chains containing generally quired to attain half saturation with oxygen, and of 145 or 146 amino acids. In man, five types of n, the exponent of the Hill equation.
    [Show full text]
  • Journal of Blood Group Serology and Molecular Genetics Volume 34, Number 1, 2018 CONTENTS
    Journal of Blood Group Serology and Molecular Genetics VOLUME 34, N UMBER 1, 2018 This issue of Immunohematology is supported by a contribution from Grifols Diagnostics Solutions, Inc. Dedicated to advancement and education in molecular and serologic immunohematology Immunohematology Journal of Blood Group Serology and Molecular Genetics Volume 34, Number 1, 2018 CONTENTS S EROLOGIC M ETHOD R EVIEW 1 Warm autoadsorption using ZZAP F.M. Tsimba-Chitsva, A. Caballero, and B. Svatora R EVIEW 4 Proceedings from the International Society of Blood Transfusion Working Party on Immunohaematology Workshop on the Clinical Significance of Red Blood Cell Alloantibodies, Friday, September 2, 2016, Dubai A brief overview of clinical significance of blood group antibodies M.J. Gandhi, D.M. Strong, B.I. Whitaker, and E. Petrisli C A S E R EPORT 7 Management of pregnancy sensitized with anti-Inb with monocyte monolayer assay and maternal blood donation R. Shree, K.K. Ma, L.S. Er and M. Delaney R EVIEW 11 Proceedings from the International Society of Blood Transfusion Working Party on Immunohaematology Workshop on the Clinical Significance of Red Blood Cell Alloantibodies, Friday, September 2, 2016, Dubai A review of in vitro methods to predict the clinical significance of red blood cell alloantibodies S.J. Nance S EROLOGIC M ETHOD R EVIEW 16 Recovery of autologous sickle cells by hypotonic wash E. Wilson, K. Kezeor, and M. Crosby TO THE E DITOR 19 The devil is in the details: retention of recipient group A type 5 years after a successful allogeneic bone marrow transplant from a group O donor L.L.W.
    [Show full text]
  • Linkage of Genes for Adult A-Globin and Embryonic Aulike Globin Chains (Hemoglobin H/Thalassemia/Embryonic Hemoglobin/Mice) J
    Proc. Natl. Acad. Sci. USA Vol. 77, No. 2, pp. 1087-1090, February 1980 Genetics Linkage of genes for adult a-globin and embryonic aulike globin chains (hemoglobin H/thalassemia/embryonic hemoglobin/mice) J. BARRY WHITNEY III* AND ELIZABETH S. RUSSELL The Jackson Laboratory, Bar Harbor, Maine 04609 contributed by Elizabeth S. Russell, November 19, 1979 ABSTRACT In a-thalassemia, the genetic locus for the a (Hbaa) female mouse and a triethylene-melamine-treated male chains of adult hemoglobin is not expressed. We have examined that carried a different, doublet, Hba haplotype (5). In this the hemoglobins of a number of individual mouse embryos affected a-thalassemic offspring of the treated male, only the heterozygous for a particular a-thalassemia (Hba th-J) and find n'o.'ecrease in the proportion of hemoglobins containing the Hbaa haplotype inherited from the C57BL/6J mother was a chain as compared to the hemoglobin containing the a-like expressed. The hemoglobins of this mouse were found by embryonic globin chain. This result suggests that the locus for electrophoresis after cystamine treatment (6) to be unusual in this embryonic a-like chain is inactivated or deleted in these that they contained a lower than normal proportion of the he- embryos as well. Because a single mutational event inactivated moglobin containing the diffuse-major:/ chain, a condition also adult and embryonic loci, we conclude that they are probably reported for the x-ray-induced mouse a-thalassemia discovered closely linked to one another on the same chromosome. We also present evidence that an unusual hemoglobin in the blood of at the Oak Ridge National Laboratory (7).
    [Show full text]
  • Comparison of Histopathology, Immunofluorescence, and Serology
    Global Dermatology Cae Report ISSN: 2056-7863 Comparison of histopathology, immunofluorescence, and serology for the diagnosis of autoimmune bullous disorders: an update Seline Ali E1, Seline Lauren N1, Sokumbi Olayemi1* and Motaparthi Kiran2,3 1Department of Dermatology, Medical College of Wisconsin, Milwaukee, WI, USA 2Dermatopathology, Miraca Life Sciences, USA 3Department of Dermatology, University of Texas Southwestern Medical Center, Dallas, TX, USA Introduction In an ELISA, the target antigen of interest (such as the NC16a domain of BP180) is immobilized by physical adsorption or by The diagnosis of autoimmune bullous disorders (AIBDs) relies on antibody capture. When antibody capture is utilized, this is referred to several different diagnostic methods. These include histopathology, as “sandwich ELISA” because the target antigen is bound between the direct immunofluorescence (DIF), indirect immunofluorescence immobilizing antibody and the primary antibody. Primary antibodies (IIF), enzyme-linked immunosorbent assay (ELISA) and are present in the patient’s serum. Enzyme-linked secondary antibodies immunoblotting. When faced with a presumptive AIBD, the are then added which bind the Fc region of primary antibodies. most widely employed method for diagnosis by dermatologists is Substrate is added and converted by the enzyme into a signal. A a combination of histopathology and DIF. While DIF is still the resulting color change, fluorescence, or electrochemical signal is diagnostic method of choice for linear IgA bullous disease and IgA quantitatively measured and reported [5]. pemphigus, ELISA is a more accurate, cost-effective and less invasive method of diagnosis for several AIBDs including pemphigus vulgaris Western blot is synonymous with immunoblot. For this method, and foliaceus, based on currently available evidence [1-3].
    [Show full text]
  • Online-Only Appendix: List of Inclusion and Exclusion Criteria
    ONLINE-ONLY APPENDIX: LIST OF INCLUSION AND EXCLUSION CRITERIA INCLUSION CRITERIA [1] Male subjects between the ages of 35 and 70 years, inclusive, with Type 2 diabetes mellitus as defined by the American Diabetes Association (Diabetes care, Vol. 21: S5- S19, 1998) for more than one year. [2] Subjects must have Body Mass Index (BMI) < 36 kg/m². [3] Stable glycemic control (Hb A1C <11%). [4] Subjects must be off all oral hypoglycemic agents 24 hours prior to each study dosing day and off any investigational drug for at least four weeks. [5] Subjects must refrain from strenuous physical activity beginning 72 hours prior to admission and through the duration of the study. [6] Subjects must be willing and able to be confined to the Clinical Research Unit as required by the protocol. [7] Subjects must be willing and able to provide written informed consent. EXCLUSION CRITERIA [1] History or presence of clinically significant cardiovascular, respiratory, hepatic, renal, gastrointestinal, neurological or infectious disorders capable of altering the absorption, metabolism or elimination of drugs, or of constituting a risk factor when taking the study medication. [2] Subjects with gastroparesis, orthostatic hypotension and hypoglycemia unawareness (autonomic neuropathy). [3] Subjects with “brittle” diabetes or predisposition to severe hypoglycemia, e.g., 2 or more serious hypoglycemic episodes (requiring another’s assistance) within the past year, or any hospitalization or emergency room visit due to poor diabetic control within the past 6 months. [4] Evidence of significant active hematological disease and/or cumulative blood donation of 1 unit (500 mL) or more including blood drawn during clinical trials in the last 3 months.
    [Show full text]
  • Egg Consumption and Human Health
    nutrients Egg Consumption and Human Health Edited by Maria Luz Fernandez Printed Edition of the Special Issue Published in Nutrients www.mdpi.com/journal/nutrients Egg Consumption and Human Health Special Issue Editor Maria Luz Fernandez MDPI • Basel • Beijing • Wuhan • Barcelona • Belgrade Special Issue Editor Maria Luz Fernandez University of Connecticut USA Editorial Office MDPI AG St. Alban-Anlage 66 Basel, Switzerland This edition is a reprint of the Special Issue published online in the open access journal Nutrients (ISSN 2072-6643) in 2015–2016 (available at: http://www.mdpi.com/journal/nutrients/special issues/egg-consumption-human-health). For citation purposes, cite each article independently as indicated on the article page online and as indicated below: Lastname, F.M.; Lastname, F.M. Article title. Journal Name. Year. Article number, page range. First Edition 2018 ISBN 978-3-03842-666-0 (Pbk) ISBN 978-3-03842-667-7 (PDF) Articles in this volume are Open Access and distributed under the Creative Commons Attribution (CC BY) license, which allows users to download, copy and build upon published articles even for commercial purposes, as long as the author and publisher are properly credited, which ensures maximum dissemination and a wider impact of our publications. The book taken as a whole is c 2018 MDPI, Basel, Switzerland, distributed under the terms and conditions of the Creative Commons license CC BY-NC-ND (http://creativecommons.org/licenses/by-nc-nd/4.0/). Table of Contents About the Special Issue Editor ...................................... v Preface to ”Egg Consumption and Human Health” .......................... vii Jose M. Miranda, Xaquin Anton, Celia Redondo-Valbuena, Paula Roca-Saavedra, Jose A.
    [Show full text]
  • Application of Quantitative Immunofluorescence to Clinical Serology: Antibody Levels of Treponema Pallidum GRACE L
    JOURNAL OF CLINICAL MICROBIOLOGY, May 1992, p. 1294-1296 Vol. 30, No. 5 0095-1137/92/051294-03$02.00/0 Copyright C 1992, American Society for Microbiology Application of Quantitative Immunofluorescence to Clinical Serology: Antibody Levels of Treponema pallidum GRACE L. PICCIOLO* AND DAVID S. KAPLAN Center for Devices and Radiological Health, Food and Drug Administration, 12200 Wilkins Avenue, Rockville, Maryland 20852 Received 27 March 1991/Accepted 20 January 1992 A previously reported method of quantitative immunofluorescence, employing a calibrated photometric system and chemically stabilized fluorescence intensity, was used to replace the subjective, visual method of endpoint determination with a quantitative, calibrated measurement of antibodies to Treponema paUlidum in serum. The results of the quantitative immunofluorescence method showed a 90% correlation with the subjective determinations of the visual method. A quantitative immunofluorescence (QIF) method to de- measured by using an acridine orange filter set, with a 400- to termine immunofluorescence with a quantitative, calibrated 440-nm excitation and LP 470 emission filters. photometric intensity of the fluorescent reaction product has Reducing agent. Dithioerythritol (DTE) (Sigma Chemical been reported previously by us (4). This method used uranyl Co., St. Louis, Mo.) was prepared as stock solution contain- glass slides in the calibration and standardization of the ing 0.3 M reducing agent in 0.5 M Tris buffer, pH 8.2 (Sigma microscope-photometer voltage measurements. To stabilize Chemical Co.). DTE was diluted 1:9 with standard buffered the fluorescence emission, dithioerythritol (DTE) was incor- glycerol mounting medium (Clinical Sciences, Inc., Whip- porated into the buffered glycerol mounting medium of the pany, N.J.) (4, 8).
    [Show full text]
  • Tangential Flow Filtration of Haptoglobin
    Received: 10 January 2020 Revised: 7 April 2020 Accepted: 21 April 2020 DOI: 10.1002/btpr.3010 RESEARCH ARTICLE Tangential flow filtration of haptoglobin Ivan S. Pires | Andre F. Palmer William G. Lowrie Department of Chemical and Biomolecular Engineering, The Ohio State Abstract University, Columbus, Ohio Haptoglobin (Hp) is a plasma glycoprotein that scavenges cell-free hemoglobin (Hb). Correspondence Hp has various potential therapeutic applications, but it has been mainly studied for *Andre F. Palmer, William G. Lowrie treatment of acute hemolytic conditions that can arise from situations such as mas- Department of Chemical and Biomolecular Engineering, The Ohio State University, sive blood transfusion, infusion of stored red blood cells, severe burns, trauma, sepsis, 151 West Woodruff Ave, Columbus, OH radiation injury, and others. Therefore, Hp may also be beneficial during chronic 43210. Email: [email protected] hemolytic disease states such as hereditary spherocytosis, nocturnal hemoglobinuria, sickle-cell anemia, and malaria. Various methods have been developed to purify Hp Funding information National Cancer Institute, Grant/Award from plasma or plasma fractions. However, none of these methods have exploited Number: P30 CA016058; National Heart, the large molecular weight (MW) range distribution of Hp polymers to easily isolate Lung, and Blood Institute, Grant/Award Numbers: R01HL126945, R01HL138116, Hp from other plasma proteins. The present study used tangential flow filtration R56HL123015; National Institute of (TFF) to isolate polymeric Hp from plasma proteins using human Fraction IV (FIV) as Biomedical Imaging and Bioengineering, Grant/ Award Number: R01EB021926; NIH Office of the starting material. After removal of insoluble material from a suspension of FIV the Director, Grant/Award Number: S10 paste, the protein mixture was clarified on a 0.2 μm hollow fiber (HF) TFF filter.
    [Show full text]
  • Life Technologies (India) Pvt. Ltd. 306, Aggarwal City Mall, Opposite M2K Pitampura, Delhi – 110034 (INDIA)
    Product Specification Sheet Chicken conalbumin (ovotransferrin) proteins Antibodies Cat # CECA15-S Rabbit Anti-Chicken conalbumin protein antiserum SIZE: 100 ul Cat # CECA15-C Chicken conalbumin protein control for Western blot SIZE: 100 ul Cat # CECA16-N Chicken conalbumin proteins SIZE: 10 mg liquid at 10 mg/ml in PBS 0.05% azide or in powder form. Allergy to chicken egg or proteins is one of the more frequent Reconstitute powder in PBS at 1-10 mg/ml. It can be used causes of food hypersensitivity in infants and young children. Both positive control for antibody #CECA15-S or for coating IgG and IgA class antibodies may be detected. Ovalbumin ELISA plates. intolerance has been implicated in a number of conditions affecting children. In particular, children with cystic fibrosis show elevated anti-ovalbumin antibodies. Ovalbumin antibodies have For Western blot +ve control (Cat # CECA15-C) is supplied also been noted in some forms of kidney disease. A relationship in SDS-PAGE sample buffer (reduced). Load 10 ul/lane of between food allergy and infantile autism has also been observed. #CECA15-C for good visibility with antibody Cat #CECA15- Children with insulin-dependent diabetes mellitus show an S. Store at –20oC in suitable size aliquots. SDS may enhanced immune response to both β-lactoglobulin and crystallize in cold conditions. It should redissolve by ovalbumin, a phenomenon that may be related to the development warming before taking it from the stock. It should be of the disease. Conditions related to ovalbumin intolerance usually heated once prior to loading on gels. If the product has resolve once egg and egg based foods have been withdrawn from been stored for several weeks, then it may be preferable to the patient's diet.
    [Show full text]
  • Conalbumin More Resistant to Proteolysis and Ther- the Use Of
    IRON AND PROTEIN KINETICS STUDIED BY MEANS OF DOUBLY LABELED HUMAN CRYSTALLINE TRANSFERRIN * BY JAY H. KATZ (From the Radioisotope and Medical Services of the Boston Veterans Administration Hospital, and the Dept. of Medicine, Boston University School of Medicine, Boston, Mass.) (Submitted for publication June 16, 1961; accepted August 10, 1961) Although proteins isotopically labeled with io- demonstrated that not only is the iron complex of dine have been used in tracer studies for some conalbumin more resistant to proteolysis and ther- years, interest has been mainly focused on their mal denaturation than the metal-free protein, but distribution and degradation in the body. While it that it is possible to maintain the iron-binding ca- is often possible to produce iodoproteins whose pacity of the former after extensive iodination. physical and chemical properties are not grossly Since both iron and transferrin levels are af- altered, the possible effects of iodination on the fected in a variety of disease states, a technique functional properties of such substances in a in which both can be followed simultaneously in physiologic setting have been less thoroughly in- vivo should prove valuable. Elmlinger and co- vestigated. That it is possible to trace label pro- workers (18) have reported in abstract form on teins without significantly reducing their biologi- the use of doubly labeled "iron-binding globulin" cal activities has been demonstrated in the case of in human subjects, but few details were given as insulin (2) and certain anterior pituitary hor- to the methods of preparation and the distribution mones (3, 4). of the two labels.
    [Show full text]
  • Clinical Placements Serology Screening for Students
    Gawler Place Medical Practice Level 1, Key Invest Building 49 Gawler Place Adelaide SA 5000 T: 08 8212 7175 F: 08 8212 1993 E: [email protected] www.adelaideunicare.com.au CLINICAL PLACEMENTS SEROLOGY SCREENING FOR STUDENTS Gawler Place Medical Practice have put together this Question and Answer sheet to assist you in meeting the requirements of SA Health’s Immunisation for Health Care Workers in South Australia Policy – August 2017. It is a requirement that all Health Care Workers have adequate immunisation against certain diseases prior to working in a clinical environment. What is Serology Screening and why do I need to do it? Serology Screening is a blood test that looks for antibodies in your blood. The purpose of such a test is to detect serum antibodies to prove protective immunity against a disease. Where can I have Serology Screening done? Gawler Place Medical Practice offer Serology Screening appointments to allow incoming students to have their serology screening completed, and where required, obtain their required vaccinations to meet SA Health’s Immunisation for Health Care Workers in South Australia – August 2017. Australian Clinical Labs are located within our Practice so that you can have your blood taken (if required) as soon as you have seen the doctor. How do I make an appointment? You may contact the practice to organise an appointment, our telephone number is 8212 7175 or make a booking online. Please make a long appointment booking. If you need to change or cancel an appointment please contact our Practice on (08) 2127175 as soon as possible so that your appointment can be offered to another person.
    [Show full text]