Relevant bibliographies by topics / Hemoglobin

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Hemoglobin'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 July 2025

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Journal articles on the topic "Hemoglobin"

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Kukačka, J., E. Klapková, and R. Průša. "Presumptive combinatory HPLC determination of fetal hemoglobin employing mode for glycated hemoglobin." Klinická biochemie a metabolismus 15, no. 3 (2007): 157–59. https://doi.org/10.61568/kbm.2007.038.

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Oshima, Minako, and Mitsuwo Hara. "Human hemoglobin and animal hemoglobins." SEIBUTSU BUTSURI KAGAKU 30, no. 3 (1986): 151–64. http://dx.doi.org/10.2198/sbk.30.151.

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Ship, Noam J., Ayça Toprak, Roseanna P. Lai, Eric Tseng, Ronald Kluger, and K. Sandy Pang. "Binding of acellular, native and cross-linked human hemoglobins to haptoglobin: enhanced distribution and clearance in the rat." American Journal of Physiology-Gastrointestinal and Liver Physiology 288, no. 6 (2005): G1301—G1309. http://dx.doi.org/10.1152/ajpgi.00399.2004.

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It is well established that hemoglobin resulting from red cell lysis binds to haptoglobin in plasma to form a complex. The increased molecular size precludes its filtration by the kidneys, redirecting it toward hepatocellular entry. Chemically cross-linked hemoglobins are designed to be resistant to renal excretion, even in the absence of haptoglobin. The manner in which binding to haptoglobin influences the pharmacokinetics of acellular cross-linked and native hemoglobins was investigated after intravenous injection of radiolabeled native human hemoglobin and trimesyl-(Lys82)β-(Lys82)β cross-
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Kozarski, Tzvetan B., Peter J. Howanitz, Joan H. Howanitz, Nenad Lilic, and Yeshpal S. Chauhan. "Blood Transfusions Leading to Apparent Hemoglobin C, S, and O-Arab Hemoglobinopathies." Archives of Pathology & Laboratory Medicine 130, no. 12 (2006): 1830–33. http://dx.doi.org/10.5858/2006-130-1830-btltah.

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Abstract Context.—Apparent hemoglobinopathies caused by blood transfusions rarely have been reported in the scientific literature. Objective.—To interpret the abnormal hemoglobins appearing as small peaks on hemoglobin chromatograms or electrophoresis membranes. Design.—In the clinical laboratories of a university hospital and a metropolitan hospital affiliated with a medical school, we interpreted hemoglobin chromatograms and electrophoresis membranes; correlated them with patients' medical, laboratory, and transfusion records; and when possible, identified the abnormal hemoglobin in the dono
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Adjé, L., V. Yapo, M. Yayo-Ayé, S. Bognini, M. Meledje, and D. Sawadogo. "Evaluation of the diagnostic accuracy of a hemoglobin S and C screening test: Sickle Scan." International Journal of Biological and Chemical Sciences 15, no. 1 (2021): 234–40. http://dx.doi.org/10.4314/ijbcs.v15i1.20.

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New tools for the rapid diagnosis of hemoglobinosis could encourage the extension of their screening in Africa. Our goal was to assess the analytical performances of a rapid hemoglobin S and C detection test, the Sickle Scan. This was a cross-sectional study carried out in March 2019 at the Yopougon Teaching Hospital. The subjects followed for hemoglobinosis as well as the subjects seeking out an electrophoresis of their hemoglobin were included. We carried out the hemogram, the electrophoresis of hemoglobin at alkaline pH (reference method) coupled with the metabisulfite sickling test (Emmel
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Edison, Eunice Sindhuvi, Ramachandran V. Shaji, Mammen Chandy, and Alok Srivastava. "Interaction of Hemoglobin E with Other Abnormal Hemoglobins." Acta Haematologica 126, no. 4 (2011): 246–48. http://dx.doi.org/10.1159/000329904.

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Smith, R. E. "A new fluorescent detection system for identifying variant hemoglobins after gel electrophoresis using immunobinding with monoclonal antibodies." Journal of Histochemistry & Cytochemistry 34, no. 5 (1986): 585–91. http://dx.doi.org/10.1177/34.5.3084625.

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This paper describes a low-resolution system for identifying variant hemoglobins with great sensitivity and specificity. After electrophoresis of the hemoglobin sample in a gel, fixation is used to entrap the hemoglobin. The gel is dried, incubated with a monoclonal antibody against the desired hemoglobin, then incubated with a second antibody against the first antibody which is conjugated with the enzyme beta-d-galactosidase. An enzyme overlay membrane containing a fluorogenic substrate is then placed on the gel surface, incubated, and removed, yielding an immunofluorescent print. The entire
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Goldman, Daniel W., Richard J. Breyer, David Yeh, Beth A. Brockner-Ryan, and Abdu I. Alayash. "Acellular hemoglobin-mediated oxidative stress toward endothelium: a role for ferryl iron." American Journal of Physiology-Heart and Circulatory Physiology 275, no. 3 (1998): H1046—H1053. http://dx.doi.org/10.1152/ajpheart.1998.275.3.h1046.

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We tested the hypothesis that chemical modifications used to produce stable, oxygen-carrying, Hb-based blood substitutes can induce cytotoxicity in endothelial cells in culture because of altered redox activity. We examined the interaction of hydrogen peroxide with nonmodified hemoglobin (HbA0) and two chemically modified hemoglobins, α-cross-linked hemoglobin (α-DBBF) and its polymerized form (poly-α-DBBF). Hydrogen peroxide-induced cell death (as assessed by lactate dehydrogenase release) in bovine aortic endothelial cells (BAEC) was completely inhibited by all three hemoglobin preparations,
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Inoguchi, Noriko, Jake R. Oshlo, Chandrasekhar Natarajan, et al. "Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix." Acta Crystallographica Section F Structural Biology and Crystallization Communications 69, no. 4 (2013): 393–98. http://dx.doi.org/10.1107/s1744309113005708.

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The deer mouse,Peromyscus maniculatus, exhibits altitude-associated variation in hemoglobin oxygen affinity. To examine the structural basis of this functional variation, the structure of the hemoglobin was solved. Recombinant hemoglobin was expressed inEscherichia coliand was purified by ion-exchange chromatography. Recombinant hemoglobin was crystallized by the hanging-drop vapor-diffusion method using polyethylene glycol as a precipitant. The obtained orthorhombic crystal contained two subunits in the asymmetric unit. The refined structure was interpreted as the aquo-met form. Structural co
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Turpeinen, U., U. H. Stenman, and R. Roine. "Liquid-chromatographic determination of acetylated hemoglobin." Clinical Chemistry 35, no. 1 (1989): 33–36. http://dx.doi.org/10.1093/clinchem/35.1.33.

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Abstract In this liquid-chromatographic assay for acetylated hemoglobin in human blood, glycated hemoglobins in hemolysates are first removed by affinity chromatography on boronate-agarose columns. Acetylated hemoglobin in the nonretained fraction is determined by cation-exchange chromatography. The absorbance of the effluent is monitored at 415 nm. The mean within-assay CV was 8.5%, the between-assay CV 17%. The mean proportion of acetylated hemoglobin in 20 pregnant, nondiabetic women was 1.9%, and in 17 alcoholics it was 2.7%. Rapid and reproducible, this method is suitable for use in routi
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Dissertations / Theses on the topic "Hemoglobin"

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Hokama, Newton Key [UNESP]. "Oxidação da hemoglobina como modelo de estudo do sistema de óxido-redução eritrocitário: interação entre nitrito de sódio, azul de metileno e cistamina." Universidade Estadual Paulista (UNESP), 2001. http://hdl.handle.net/11449/102659.

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Made available in DSpace on 2014-06-11T19:32:13Z (GMT). No. of bitstreams: 0 Previous issue date: 2001Bitstream added on 2014-06-13T19:42:37Z : No. of bitstreams: 1 hokama_nk_dr_botfm.pdf: 442709 bytes, checksum: 19c729c7bb99de9b488b0c496f8b3922 (MD5)<br>A hemoglobina, o componente principal do citoplasma eritrocitário, está sujeita à oxidação, fisiologicamente ou por agentes externos, seja através da formação de Metahemoglobina, ou pela oxidação da cisteína β93 por agentes tiois. Impossibilitado de sintetizar proteína, o eritrócito depende primordialmente da via glicolítica, que, além de fo
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Žilytė, Diana. "Cukrinio diabeto monitoravimo laboratorinių rodiklių metodologinė analizė." Master's thesis, Lithuanian Academic Libraries Network (LABT), 2014. http://vddb.library.lt/obj/LT-eLABa-0001:E.02~2006~D_20140702_193728-67988.

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Daug pasaulinių organizacijų, kurios stengiasi pagerinti cukrinio diabeto diagnostiką ir sergančių pacientų glikemijos kontrolę, nes nepakankama ir vėlyva diagnostika skatina komplikacijų atsiradimą ir progresavimą. Šio darbo tikslas išanalizuoti cukriniu diabetu sergančių pacientų metodologinių ypatumų įtaką glikozilinto hemoglobino rezultatams. Išmatavus analitę HbA1c, 100 pacientų sergančių cukriniu diabetu, trimis skirtingos standartizacijos analizinėmis sistemomis Roche-Hitachi 917, Bayer-Advia1650 ir Dade Behring-Dimension RxL, gauta koreliacija su trijų mėnesių gliukozės koncentracijos
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Hokama, Newton Key. "Oxidação da hemoglobina como modelo de estudo do sistema de óxido-redução eritrocitário : interação entre nitrito de sódio, azul de metileno e cistamina /." Botucatu : [s.n.], 2001. http://hdl.handle.net/11449/102659.

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Orientador: Luiz Shiguero Matsubara<br>Resumo: A hemoglobina, o componente principal do citoplasma eritrocitário, está sujeita à oxidação, fisiologicamente ou por agentes externos, seja através da formação de Metahemoglobina, ou pela oxidação da cisteína β93 por agentes tiois. Impossibilitado de sintetizar proteína, o eritrócito depende primordialmente da via glicolítica, que, além de fornecer ATP, através da integração da formação de NADH e da Via da Hexose Monofosfato, mantém o potencial redutor extremamente eficiente. A presente investigação teve como finalidade avaliar o sistema de óxido-r
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kolagatla, sandhya, nagabhishek moka, and samuel bailey. "FAMILIAL POLYCYTHEMIA LIKELY DUE TO NOVEL HEMOGLOBIN VARIANT- HEMOGLOBIN HYDEN." Digital Commons @ East Tennessee State University, 2018. https://dc.etsu.edu/asrf/2018/schedule/89.

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Adult hemoglobin (HbA) is made up of two pairs of globin chains. Some rare mutations of the globin chains can result in high affinity towards hemoglobin molecule thus changing the equilibrium of normal oxygen loading in lungs and the delivery of same to the tissues. Because of change in the affinity to the oxygen these mutations can result in erythrocytosis (polycythemia). Here we discuss a case of Familial Polycythemia likely due to novel hemoglobin variant. 42-year Caucasian male presents to the clinic with high hemoglobin for several years but otherwise denies any symptoms of headache, visi
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Lock-O'Brien, Jodi J. L. "Hemoglobin bis-tetramers, synthesis of cross-linker and reaction with hemoglobin." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp04/mq29226.pdf.

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Ramos, Lierge [UNESP]. "Estudos biofísicos da Hemoproteína extracelular de Amynthas gracilis (HbAg) na ausência e na presença de surfactantes." Universidade Estadual Paulista (UNESP), 2017. http://hdl.handle.net/11449/151572.

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Submitted by LIERGE RAMOS null (lrg.ramos@hotmail.com) on 2017-09-06T20:31:40Z No. of bitstreams: 1 Lierge_Ramos_Dissertação_Biotecnologia.2017.pdf: 2068937 bytes, checksum: 107fae4a7bea607b2de9a6fd531de01f (MD5)<br>Approved for entry into archive by Monique Sasaki (sayumi_sasaki@hotmail.com) on 2017-09-11T19:41:07Z (GMT) No. of bitstreams: 1 ramos_l_me_araiq.pdf: 2068937 bytes, checksum: 107fae4a7bea607b2de9a6fd531de01f (MD5)<br>Made available in DSpace on 2017-09-11T19:41:07Z (GMT). No. of bitstreams: 1 ramos_l_me_araiq.pdf: 2068937 bytes, checksum: 107fae4a7bea607b2de9a6fd531de01f (MD5)
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Miyashiro, Samantha Ive. "Caracterização fenotípica do camundongo BALB/c mutante anêmico." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/10/10133/tde-29042013-155003/.

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Várias linhagens de camundongos resultam de mutações genéticas pontuais espontâneas ou induzidas e estas alterações podem apresentar fenótipos relevantes semelhantes a doenças hereditárias humanas. Massironi et al. (2006) desenvolveram vários camundongos BALB/c mutantes com o agente mutagênico etil-nitroso-uréia (ENU) no Biotério de Experimentação do Departamento de Imunologia do Instituto de Ciências Biomédicas (ICB) da Universidade de São Paulo. Destes, o mutante chamado anêmico foi objeto de estudo desta pesquisa, que tem como objetivo a sua fenotipagem. A avaliação hematológica revelou mod
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Jorge, Susan Elisabeth Domingues Costa 1983. "Correlação estrutura-função de variantes da hemoglobina humana = Structure-function relations of human hemoglobin variants." [s.n.], 2013. http://repositorio.unicamp.br/jspui/handle/REPOSIP/310885.

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Orientadores: Maria de Fatima Sonati, Munir Salomão Skaf<br>Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Ciências Médicas<br>Made available in DSpace on 2018-08-23T23:13:39Z (GMT). No. of bitstreams: 1 Jorge_SusanElisabethDominguesCosta_D.pdf: 8714965 bytes, checksum: 3191d67be1e9be2f9782ce3483bcfd3a (MD5) Previous issue date: 2013<br>Resumo: O resumo poderá ser visualizado no texto completo da tese digital<br>Abstract: The complete abstract is available with the full electronic document<br>Doutorado<br>Ciencias Biomedicas<br>Doutora em Ciências Médicas
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Teytelboym, Anna. "Tetrafunctional cross-linking reagents, reaction with hemoglobin and the formation of hemoglobin bis-tetramers." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0001/MQ45932.pdf.

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Croci, Simonetta. "Conformational changes in hemoglobin triggered by changing the iron charge, high and low affinity hemoglobin." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=980529441.

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Books on the topic "Hemoglobin"

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Nagel, Ronald L. Hemoglobin Disorders. Humana Press, 2003. http://dx.doi.org/10.1385/1592593739.

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Honig, George R., and Junius G. Adams. Human Hemoglobin Genetics. Springer Vienna, 1986. http://dx.doi.org/10.1007/978-3-7091-8798-2.

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1943-, Adams Junius G., ed. Human hemoglobin genetics. Springer-Verlag, 1986.

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Honig, George R. Human hemoglobin genetics. Springer-Verlag, 1985.

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Di Prisco, G., B. Giardina, and R. E. Weber. Hemoglobin Function in Vertebrates. Springer Milan, 2000. http://dx.doi.org/10.1007/978-88-470-2111-2.

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Spahn, Marge A. Hemoglobin and microhematocrit determinations. 3rd ed. Kettering Medical Center, School of Medical Technology, 1992.

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Spahn, Marge A. Hemoglobin and microhematocrit determinations. 3rd ed. Kettering Medical Center, School of Medical Technology, 1992.

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International, Symposium on Stabilized Hemoglobin (1986 Tokyo Japan). International Symposium on Stabilized Hemoglobin. ISAO Press, 1987.

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George, Stamatoyannopoulos, Nienhuis Arthur W, and Conference on Hemoglobin Switching (7th : 1990 : Airlie, Va.), eds. The Regulation of hemoglobin switching. Johns Hopkins University Press, 1991.

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Bodensee Symposium on Microcirculation (17th 2002 Lindau, Bavaria, Germany). Microcirculatory effects of hemoglobin solutions. Edited by Messmer K, Burhop K. E, and Hutter J. Karger, 2004.

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Book chapters on the topic "Hemoglobin"

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Gupta, Anil. "Hemoglobin." In Comprehensive Biochemistry for Dentistry. Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-1035-5_5.

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Zasler, Nathan D. "Hemoglobin." In Encyclopedia of Clinical Neuropsychology. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-57111-9_39.

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Zasler, Nathan D. "Hemoglobin." In Encyclopedia of Clinical Neuropsychology. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-56782-2_39-2.

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Barisas, B. George. "Hemoglobin." In Thermodynamic Data for Biochemistry and Biotechnology. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71114-5_9.

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Sainburg, Robert L., Andrew L. Clark, George E. Billman, et al. "Hemoglobin." In Encyclopedia of Exercise Medicine in Health and Disease. Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2479.

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McGrath, Marie C. "Hemoglobin." In Encyclopedia of Child Behavior and Development. Springer US, 2011. http://dx.doi.org/10.1007/978-0-387-79061-9_1348.

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Gooch, Jan W. "Hemoglobin." In Encyclopedic Dictionary of Polymers. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13894.

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Zasler, Nathan D. "Hemoglobin." In Encyclopedia of Clinical Neuropsychology. Springer New York, 2011. http://dx.doi.org/10.1007/978-0-387-79948-3_39.

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Goldberg, Daniel E., and Philip J. Rosenthal. "Hemoglobin Digestion." In Encyclopedia of Malaria. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-8757-9_7-1.

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Patrinos, George P., and Stylianos E. Antonarakis. "Human Hemoglobin." In Vogel and Motulsky's Human Genetics. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-37654-5_13.

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Conference papers on the topic "Hemoglobin"

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Cheburkanov, Vsevolod, Mykyta Kizilov, and Vladislav Yakovlev. "Fluorescence lifetime spectroscopy of hemoglobin." In Optical Diagnostics and Sensing XXV: Toward Point-of-Care Diagnostics, edited by Justin S. Baba and Gerard L. Coté. SPIE, 2025. https://doi.org/10.1117/12.3044088.

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C, Manimaran, Neeharika S, Neelambari R. A, and Nirmala K. "Non-Invasive Frequent Hemoglobin Monitoring System." In 2025 International Conference on Wireless Communications Signal Processing and Networking (WiSPNET). IEEE, 2025. https://doi.org/10.1109/wispnet64060.2025.11005029.

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Saeed, Fiza, Caroline Carter, John Kolade, Robert Matthew Brothers, and Hanli Liu. "Depth-resolved metabolic responses to forearm arterial occlusion measured with two-channel broadband NIRS." In Optics and the Brain. Optica Publishing Group, 2025. https://doi.org/10.1364/brain.2025.btu4b.2.

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This study used 2-channel broadband near-infrared spectroscopy (bbNIRS) to measure tissue responses during forearm arterial occlusion. While oxy-hemoglobin concentration decreased and deoxy-hemoglobin concentration increased, oxidized cytochrome c oxidase concentration remained unchanged, indicating sustained mitochondrial metabolism.
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M, Jayasanthi, Vismitha V, and Eunice Joshi A P. "A Non-Invasive Approach for Hemoglobin Estimation." In 2024 International Conference on Smart Systems for Electrical, Electronics, Communication and Computer Engineering (ICSSEECC). IEEE, 2024. http://dx.doi.org/10.1109/icsseecc61126.2024.10649469.

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Saini, Surendra Kumar, Sakshi Tiwari, Anil Sharma, and Ravi Kumar Maddila. "Estimation of Glycated Hemoglobin Using Multiwavelength Photoplethysmography Signal." In 2024 IEEE Region 10 Symposium (TENSYMP). IEEE, 2024. http://dx.doi.org/10.1109/tensymp61132.2024.10752123.

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Topunov, A. F., O. V. Kosmachevskaya, and O. E. Bagrova. "ENZYMATIC SYSTEMS FOR REDUCTION OF HEMOGLOBINS." In NOVEL TECHNOLOGIES IN MEDICINE, BIOLOGY, PHARMACOLOGY AND ECOLOGY. LLC Institute Information Technologies, 2024. http://dx.doi.org/10.47501/978-5-6044060-4-5.73-77.

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The view on the reductase systems supporting hemoglobin in physiologically active reduced state is providing. The existence of such reductase systems is essential for functioning of all hemoglobins. They can be special reductases, reductase domains, connected with globin molecule, and reductas-es of wide spectrum of activitie for which reduction of hemoglobin is one of possible functions.
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Wu, Tao, Ye Yang, X. Sheldon Wang, et al. "A Molecular Dynamic Modeling of Hemoglobin-Hemoglobin Interactions." In PROCEEDINGS OF THE 2ND INTERNATIONAL SYMPOSIUM ON COMPUTATIONAL MECHANICS AND THE 12TH INTERNATIONAL CONFERENCE ON THE ENHANCEMENT AND PROMOTION OF COMPUTATIONAL METHODS IN ENGINEERING AND SCIENCE. AIP, 2010. http://dx.doi.org/10.1063/1.3452299.

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Abbasi, Sara, Bastián Carnero Groba, Ilse Weets, et al. "SERS biosensing of sickle cell hemoglobin from normal hemoglobin." In Enhanced Spectroscopies and Nanoimaging 2023, edited by Prabhat Verma and Yung Doug Suh. SPIE, 2023. http://dx.doi.org/10.1117/12.2675806.

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Kessler, Manfred D., Alfons Krug, Juergen Spaeth, S. Aigner, and M. Batz. "Intensity of intracapillary hemoglobin remission spectra as a function of hemoglobin concentration." In International Symposium on Biomedical Optics Europe '94, edited by Sigrid Avrillier, Britton Chance, Gerhard J. Mueller, Alexander V. Priezzhev, and Valery V. Tuchin. SPIE, 1995. http://dx.doi.org/10.1117/12.200832.

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Franceschini, Maria Angela, Sergio Fantini, Albert Cerussi, Beniamino Barbieri, Britton Chance, and Encico Gratton. "The Effect of Water in the Quantitation of Hemoglobin Concentration in a Tissue-Like Phantom by Near-Infrared Spectroscopy." In Biomedical Optical Spectroscopy and Diagnostics. Optica Publishing Group, 2006. http://dx.doi.org/10.1364/bosd.1996.ap16.

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We have investigated the contribution of water in the quantitative determination of hemoglobin concentration and saturation by near-infrared spectroscopy in turbid media. Our study consists of in vitro measurements on an aqueous suspension containing Liposyn, bovine blood, and yeast, buffered at pH 7.2. The optical coefficients of the medium (μ a ,~0.03-0.08 cm−1, μ s ′ ~0 cm−1) match those of biological tissue in the near-infrared, and the hemoglobin concentration (23 μM) is also similar to that found in tissues. We were able to reversibly saturate and desaturate hemoglobin in the full range
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Reports on the topic "Hemoglobin"

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Tye, Ross W. Stabilized Hemoglobin Wound Healing Development. Defense Technical Information Center, 2012. http://dx.doi.org/10.21236/ada612551.

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Manning, James M. Carboxyalkylated Hemoglobin as a Potential Blood Substitute. Defense Technical Information Center, 1991. http://dx.doi.org/10.21236/ada252329.

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Manning, James M. Carboxyalkylated Crosslinked Hemoglobin as a Potential Blood Substitute. Defense Technical Information Center, 1995. http://dx.doi.org/10.21236/ada296762.

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Manning, James M. Carboxyalkylated Crosslinked Hemoglobin as a Potential Blood Substitute. Defense Technical Information Center, 1996. http://dx.doi.org/10.21236/ada306017.

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Ostrowski, Stanislaw, Thomas G. Burke, and Waldemar Priebe. 13 C NMR Spectra of Allosteric Effectors of Hemoglobin. Defense Technical Information Center, 1993. http://dx.doi.org/10.21236/ada262979.

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Logue, B. A., B. J. Pieper, and S. D. Royster-Cunningham. Investigation of Soman Adducts of Human Hemoglobin by Liquid Chromatography. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada443087.

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Phillips, William T. In Vivo Distribution of Liposome Encapsulated Hemoglobin Studied with Imaging Radiotracers. Defense Technical Information Center, 1993. http://dx.doi.org/10.21236/ada262533.

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Burke, Thomas G. Evaluation of Liposome-Encapsulated Hemoglobin/LR16 Formulation as a Potential Blood Substitute. Defense Technical Information Center, 1991. http://dx.doi.org/10.21236/ada233973.

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Burke, Thomas G. Evaluation of Liposome-Encapsulated Hemoglobin/LR16 Formulations as a Potential Blood Substitute. Defense Technical Information Center, 1991. http://dx.doi.org/10.21236/ada243075.

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Burke, Thomas G. Evaluation of Liposome-Encapsulated Hemoglobin/LR16 Formulations as a Potential Blood Substitute. Defense Technical Information Center, 1991. http://dx.doi.org/10.21236/ada244806.

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