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Journal articles on the topic 'Hemoglobin'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Moscoso, H., C. R. Kiefer, A. Kutlar, and F. A. Garver. "Quantification of hemoglobins S, C, and F by a magnetic affinity immunoassay." Clinical Chemistry 34, no. 5 (1988): 902–5. http://dx.doi.org/10.1093/clinchem/34.5.902.

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Abstract This magnetic affinity immunoassay (MAIA) quantifies hemoglobins (Hb) S, C, and F in hemolysates from adults or newborns. Monospecific antisera to the hemoglobins are covalently conjugated to magnetic beads and reacted with the corresponding 125I-labeled hemoglobin. After centrifugation to separate the free and antibody-bound 125I-labeled hemoglobin, the amount of radioactive hemoglobin in the pellet is measured. To determine the concentration of the Hb under study, the percent inhibition of the reaction is quantified. The standard curve is established by adding known quantities of un

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12

Little, Randie R., and William L. Roberts. "A Review of Variant Hemoglobins Interfering with Hemoglobin A1c Measurement." Journal of Diabetes Science and Technology 3, no. 3 (2009): 446–51. http://dx.doi.org/10.1177/193229680900300307.

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Hemoglobin A1c (HbA1c) is used routinely to monitor long-term glycemic control in people with diabetes mellitus, as HbA1c is related directly to risks for diabetic complications. The accuracy of HbA1c methods can be affected adversely by the presence of hemoglobin (Hb) variants or elevated levels of fetal hemoglobin (HbF). The effect of each variant or elevated HbF must be examined with each specific method. The most common Hb variants worldwide are HbS, HbE, HbC, and HbD. All of these Hb variants have single amino acid substitutions in the Hb β chain. HbF is the major hemoglobin during intrau

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13

Bissé, E., P. Huaman-Guillen, and H. Wieland. "Chromatographic evaluation of minor hemoglobins: clinical significance of hemoglobin A1d, comparison with hemoglobin A1c, and possible interferences." Clinical Chemistry 41, no. 5 (1995): 658–63. http://dx.doi.org/10.1093/clinchem/41.5.658.

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Abstract Using an HPLC procedure, we evaluated &gt; 10 minor hemoglobins (Hbs) in healthy adults, individuals on long-term aspirin therapy, diabetic subjects, and uremic patients. Hb A1c and Hb A1d3 were the most abundant and important minor Hb components, respectively, accounting for 4.10% +/- 0.50% and 3.46% +/- 0.43% of total Hb in 361 healthy subjects. Acetylated Hb A was a potential interferent in the measurement of Hb A1c. The amounts of both Hb A1d3 and Hb A1carb were significantly increased in uremic patients, indicating that these Hb adducts may be carbamylated. There was a signif

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14

Rohde, Kyle H., and David W. Dyer. "Analysis of Haptoglobin and Hemoglobin-Haptoglobin Interactions with the Neisseria meningitidis TonB-Dependent Receptor HpuAB by Flow Cytometry." Infection and Immunity 72, no. 5 (2004): 2494–506. http://dx.doi.org/10.1128/iai.72.5.2494-2506.2004.

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ABSTRACT Neisseria meningitidis expresses a two-component TonB-dependent receptor, HpuAB, which mediates heme-iron (Hm-Fe) acquisition from hemoglobin and hemoglobin-haptoglobin complexes. Due to genetic polymorphisms in the human haptoglobin gene, haptoglobin (and hemoglobin-haptoglobin) exists as three structurally distinct phenotypes. In this study, we examined the influence of the haptoglobin phenotype on the interactions of HpuAB with apo-haptoglobin and hemoglobin-haptoglobin. Growth assays confirmed that HpuAB utilizes hemoglobin-haptoglobin more efficiently than hemoglobin as an Fe sou

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15

Jhiang, Sissy M., James R. Garey, and Austen F. Riggs. "Exon-Intron Organization in Genes of Earthworm and Vertebrate Globins." Science 240, no. 4850 (1988): 334–36. http://dx.doi.org/10.1126/science.2832953.

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The structure of an invertebrate, intron-containing globin gene has been determined as part of a study of the evolution of hemoglobin. The gene encoding chain c of Lumbricus terrestris hemoglobin has the two-intron, three-exon structure characteristic of vertebrate globin genes, and the exact positions of the splice junctions are conserved. The two introns interrupting the coding sequence are longer than those of known hemoglobins but shorter than myoglobin introns. The gene encodes a secretory preglobin containing a 16-residue signal peptide, as expected for an extracellular hemoglobin. Howev

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16

Lamba, S. S., B. A. Bricker, K. Y. Buch, and H. Lewis, Ill. "Use of Commercially Available Hemoglobin Standards to Quantitatively Calibrate a High Performance Liquid Chromatography Method." Current Medicinal Chemistry 5, no. 1 (1998): 63–72. http://dx.doi.org/10.2174/0929867305666220314195610.

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High performance liquid chromatography (HPLC) has proven to be an extremely useful analytical technique to separate and identify different types of hemoglobins, particularly A, C, F and S in blood samples, and compute their relative percentages. Such data provide useful information in the diagnosis of hemoglobinopathies including sickle cell anemia, β -thalassemia, hemoglobin C disease,etc. In the present investigation, we have explored the determination of absolute concentrations of individual hemoglobins in g/dal nd recommend it as an additional parameter which could be included .as part of

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17

Hill, Robert D. "What are hemoglobins doing in plants?" Canadian Journal of Botany 76, no. 5 (1998): 707–12. http://dx.doi.org/10.1139/b98-057.

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Within the last 3-4 years, evidence has accumulated to indicate that hemoglobin proteins exist widely in the plant community. This review presents some of the evidence to support this view and describes some of the properties of a barley hemoglobin. Barley hemoglobin has a strong avidity for oxygen, having an oxygen dissociation constant for oxyhemoglobin of 3 nmol L-1. It is induced under low oxygen tensions, with the induction regulated by ATP, or some consequence of ATP action. Experiments with transformed maize cells indicate that hemoglobin acts to improve the energy status of plant cells

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18

Bunn, HF. "Subunit assembly of hemoglobin: an important determinant of hematologic phenotype." Blood 69, no. 1 (1987): 1–6. http://dx.doi.org/10.1182/blood.v69.1.1.1.

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Abstract Hemoglobin's physiologic properties depend on the orderly assembly of its subunits in erythropoietic cells. The biosynthesis of alpha- and beta-globin polypeptide chains is normally balanced. Heme rapidly binds to the globin subunit, either during translation or shortly thereafter. The formation of the alpha beta-dimer is facilitated by electrostatic attraction of a positively charged alpha-subunit to a negatively charged beta-subunit. The alpha beta-dimer dissociates extremely slowly. The difference between the rate of dissociation of alpha beta- and alpha gamma-dimers with increasin

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19

Bunn, HF. "Subunit assembly of hemoglobin: an important determinant of hematologic phenotype." Blood 69, no. 1 (1987): 1–6. http://dx.doi.org/10.1182/blood.v69.1.1.bloodjournal6911.

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Hemoglobin's physiologic properties depend on the orderly assembly of its subunits in erythropoietic cells. The biosynthesis of alpha- and beta-globin polypeptide chains is normally balanced. Heme rapidly binds to the globin subunit, either during translation or shortly thereafter. The formation of the alpha beta-dimer is facilitated by electrostatic attraction of a positively charged alpha-subunit to a negatively charged beta-subunit. The alpha beta-dimer dissociates extremely slowly. The difference between the rate of dissociation of alpha beta- and alpha gamma-dimers with increasing pH expl

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20

Frontice, Clara, Gary L. Gilliland, Gregory B. Vasquez, Xinhua Ji та Igor Pechik. "Oxygen Binding to α-Subunits in High-Salt Crystals of t-State Hemoglobin". Protein & Peptide Letters 6, № 2 (1999): 59–66. http://dx.doi.org/10.2174/092986650602221108150658.

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Abstract: The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β (C93A+C 112G), have been determined at 2.0 A and 1.8 A resolution, respectively. Oxygen molecules fully occupy the, α -heme and partially occupy the a.,-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.

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21

Adewoyin, Ademola, Olusogo Busari, and Oladapo Aworanti. "Hemoglobin Phenotypes in Nigeria: Data From a National Reference Laboratory." American Journal of Clinical Pathology 152, Supplement_1 (2019): S115—S116. http://dx.doi.org/10.1093/ajcp/aqz121.027.

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Abstract On a global scale, 5% to 7% of the population carries an abnormal hemoglobin. With a sickle hemoglobin (HbS) carrier prevalence of 25% to 40%, Nigeria bears the greatest burden of sickle cell disorder worldwide. Until recent times, detection of other clinically significant hemoglobin variants associated with HbS has been unavailable, resulting in missed/wrong diagnosis, weak national data, and suboptimal control of hemoglobin disorders. This study aimed to review hemoglobin assays over a 2-year period at a national reference laboratory in Nigeria, in order to describe the prevalent he

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22

Scrima, Rosella, Sabino Fugetto, Nazzareno Capitanio, and Domenico L. Gatti. "On the Origin of Hemoglobin Cooperativity under Non-equilibrium Conditions." Discoveries 10, no. 2 (2022): e146. http://dx.doi.org/10.15190/d.2022.5.

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Abnormal hemoglobins can have major consequences for tissue delivery of oxygen. Correct diagnosis of hemoglobinopathies with altered oxygen affinity requires a determination of hemoglobin oxygen dissociation curve, which relates the hemoglobin oxygen saturation to the partial pressure of oxygen in the blood. Determination of the oxygen dissociation curve of human hemoglobin is typically carried out under conditions in which hemoglobin is in equilibrium with O2 at each partial pressure. However, in the human body due to the fast transit of red blood cells through tissues hemoglobin oxygen excha

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23

Bard, Harry, and Janie Prosmanne. "Relative Rates of Fetal Hemoglobin and Adult Hemoglobin Synthesis in Cord Blood of Infants of Insulin-Dependent Diabetic Mothers." Pediatrics 75, no. 6 (1985): 1143–47. http://dx.doi.org/10.1542/peds.75.6.1143.

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Erythrocytosis, extramedullary erythropoiesis, and increased levels of plasma erythropoietin have been observed in newborn infants of diabetic mothers. Because there is evidence that there is a relationship between increased fetal hemoglobin production and acute erythropoietic expansion, it was considered important to study the proportion of fetal hemoglobin and adult hemoglobin synthesis in newborn infants of insulin-dependent diabetic mothers. Samples from nine newborn infants of diabetic mothers as well as nine control infants, ranging from 36 to 38 weeks of gestation, were incubated in an

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24

Cane, Roy D. "Hemoglobin." Critical Care Medicine 18, no. 9 (1990): 1046. http://dx.doi.org/10.1097/00003246-199009000-00028.

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25

Huehns, E. R. "Hemoglobin." FEBS Letters 180, no. 1 (1985): 130. http://dx.doi.org/10.1016/0014-5793(85)80249-0.

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26

Bergstrom, Richard W. "Fetal Hemoglobin Alters Hemoglobin A_1c Measurements." Annals of Internal Medicine 115, no. 8 (1991): 656. http://dx.doi.org/10.7326/0003-4819-115-8-656_1.

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27

Kuchay, MohammadShafi, Ambrish Mithal, and Niharika Yedla. "Hemoglobin E disease and glycosylated hemoglobin." Indian Journal of Endocrinology and Metabolism 19, no. 5 (2015): 683. http://dx.doi.org/10.4103/2230-8210.163211.

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28

Kluger, Ronald. "2001 Lemieux Award Lecture Organic chemistry and hemoglobin: Benefits from controlled alteration." Canadian Journal of Chemistry 80, no. 3 (2002): 217–21. http://dx.doi.org/10.1139/v01-200.

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Hemoglobin carries oxygen in circulation within red cells but does not function outside the cells because it fails not only to release oxygen but also dissociates into dimers that make up the tetrameric protein. Bifunctional anionic acylating agents that contain a structurally rigid bridge introduce cross-links that stabilize hemoglobin and alter its oxygen affinity so that it could be used to carry oxygen outside cells. Nitric oxide binds to hemoglobin and in circulation this causes undesirable increases in blood pressure. It had been reported that higher weight collections of hemoglobin do n

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29

Lailla, Meimi, Z. Zainar, and Ade Fitri. "Perbandingan Hasil Pemeriksaan Hemoglobin Secara Digital Terhadap Hasil Pemeriksaan Hemoglobin Secara Cyanmethemoglobin." Jurnal Pengelolaan Laboratorium Pendidikan 3, no. 2 (2021): 63–68. http://dx.doi.org/10.14710/jplp.3.2.63-68.

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Background: Various methods of hb examination are used by health facilities in Indonesia. Examinations with auto analyzers that use the cyanmethemoglobin method are proven to be accurate and produce reliable measurements. A practical and easy to do hemoglobin check is the digital method (Hb meter). This study aims to determine the differences in the results of digital hb examination using capillary blood with the cyanmethemoglobin method using venous blood.Methods: This study is a comparative study using primary data. There were 30 respondents who were randomly taken in the Clinical Pathology

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30

Bellelli, Andrea, and Maurizio Brunori. "Control of Oxygen Affinity in Mammalian Hemoglobins: Implications for a System Biology Description of the Respiratory Properties of the Red Blood Cell." Current Protein & Peptide Science 21, no. 6 (2020): 553–72. http://dx.doi.org/10.2174/1389203721666200203151414.

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Hemoglobin and myoglobin have been considered for a long time the paradigmatic model systems for protein function, to the point of being defined the “hydrogen atom[s] of biology”. Given this privileged position and the huge amount of quantitative information available on these proteins, the red blood cell might appear as the model system and“hydrogen atom” of system biology. Indeed, since the red cell&#039;s main function is O2 transport by hemoglobin, the gap between the protein and the cell may appear quite small. Yet, a surprisingly large amount of detailed biochemical information is re

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31

Cruz, Daiana Márcia Melo, Seyna Ueno Rabelo Mendes, and Bruno Sousa Pires. "Doença falciforme e o acompanhamento na atenção básica: relato de caso." Revista de Patologia do Tocantins 4, no. 3 (2017): 47. http://dx.doi.org/10.20873/uft.2446-6492.2017v4n3p47.

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No presente relato os autores descrevem um caso de Doença Falciforme em uma criança de 04 anos de idade destacando a importância do seu acompanhamento pela atenção básica. Essa doença decorre de uma mutação no gene que produz a hemoglobina A, originando outra, denominada hemoglobina S, de herança recessiva. O curso clínico é o de uma doença falciforme de intensidade menos grave. As crises hemolíticas são mais amenas. O baço está aumentado na criança, poedendo persistir na idade adulta. Além disso, há perda da função esplênica de forma gradual. O diagnóstico é realizado através da Eletroforese

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32

Wilber, Andrew, Arthur W. Nienhuis, and Derek A. Persons. "Transcriptional regulation of fetal to adult hemoglobin switching: new therapeutic opportunities." Blood 117, no. 15 (2011): 3945–53. http://dx.doi.org/10.1182/blood-2010-11-316893.

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Abstract In humans, embryonic, fetal, and adult hemoglobins are sequentially expressed in developing erythroblasts during ontogeny. For the past 40 years, this process has been the subject of intensive study because of its value to enlighten the biology of developmental gene regulation and because fetal hemoglobin can significantly ameliorate the clinical manifestations of both sickle cell disease and β-thalassemia. Understanding the normal process of loss of fetal globin expression and activation of adult globin expression could potentially lead to new therapeutic approaches for these hemoglo

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33

Wang, Qijun, Xiaoheng Zhao, Yunlong Liu, et al. "Characterization and Expression Analysis of Genes from Megalobrama amblycephala Encoding Hemoglobins with Extracellular Microbicidal Activity." Genes 14, no. 10 (2023): 1972. http://dx.doi.org/10.3390/genes14101972.

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Hemoglobin (Hb) usually comprises two α and two β subunits, forming a tetramer responsible for oxygen transportation and storage. Few studies have elucidated fish hemoglobin immune functions. Megalobrama amblycephala is a freshwater-cultured fish prevalent in China. We identified two M. amblycephala hemoglobin subunits and analyzed their expression patterns and antibacterial activities. The respective full-length cDNA sequences of the M. amblycephala Hb α (MaHbα) and β (MaHbβ) subunits were 588 and 603 bp, encoding 143 and 148 amino acids. MaHbα and MaHbβ were highly homologous to hemoglobins

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34

Watts, R. A., P. W. Hunt, A. N. Hvitved, M. S. Hargrove, W. J. Peacock, and E. S. Dennis. "A hemoglobin from plants homologous to truncated hemoglobins of microorganisms." Proceedings of the National Academy of Sciences 98, no. 18 (2001): 10119–24. http://dx.doi.org/10.1073/pnas.191349198.

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35

Agesti, Nireza, Damrah Damrah, Willadi Rasyid, Wilda Welis, Dally Rahman, and Fiky Zarya. "The Role of Hemoglobin in Maintaining Health: A Literature Review." JURNAL INFO KESEHATAN 22, no. 2 (2024): 395–408. http://dx.doi.org/10.31965/infokes.vol22.iss2.1482.

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The role of hemoglobin in maintaining health is still not fully understood Thoroughly. Therefore, this literature review aims to uncover comprehensively the role of hemoglobin in maintaining health. Objective: The purpose of this literature review is to investigate the role of hemoglobin in maintaining health by collecting and analyzing current findings in the scientific literature. The methodology used is a systematic search through academic databases such as PubMed, Google Scholar, and Scopus using relevant keywords such as "hemoglobin", "health maintenance", and "literature review". Article

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36

Putri, Shafira Maulani, Efrida ., and Hudila Rifa Karmia. "Relationship of Protein Intake with Hemoglobin and Reticulocyte Hemoglobin Levels in Pregnant Women." International Journal of Research and Review 10, no. 7 (2023): 87–92. http://dx.doi.org/10.52403/ijrr.20230714.

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Anemia in pregnant women is a big problem in Indonesia, including West Sumatra. In the city of Padang, the provincial capital and the largest city in West Of the 23 Puskesmas in Padang City, the highest cases of anemia in pregnant women were recorded at the Pauh Puskesmas, which was 20%. One of the important causes of anemia is iron deficiency in the body of pregnant women. Iron deficiency during pregnancy occurs due to a doubling of the need for iron caused by an increase in blood volume to meet the mother's needs and the fetus's growth during pregnancy. Protein is the structure of hemoglobin

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37

Baranowska-Jaźwiecka, Anna Iza, Beata Mianowska, Wojciech Fendler, Agnieszka Pomykała, and Wojciech Młynarski. "Fetal hemoglobin and hemoglobin A1c level among pediatric patients with type 1 diabetes." Pediatric Endocrinology Diabetes and Metabolism 22, no. 2 (2016): 48–53. http://dx.doi.org/10.18544/pedm-22.02.0050.

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38

Balaka, Kemal Idris, Heni Umar, and Niar Jumiarti Saadi. "GAMBARAN KADAR HEMOGLOBIN DAN INDEKS ERITROSIT SEBAGAI PENANDA ANEMIA PADA KARYAWAN PT. ANTAM DI KECAMATAN POMALAA KABUPATEN KOLAKA PROVINSI SULAWESI TENGGARA." Jurnal Analis Kesehatan Kendari 6, no. 1 (2023): 6–10. http://dx.doi.org/10.46356/jakk.v6i1.282.

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ABSTRACT Anemia is a condition in which the hemoglobin (Hb) level in the blood is less than normal. Anemia is a nutritional problem that is widely found throughout the world that not only occurs in developing countries but also in developed countries Anemia is a condition with hemoglobin levels, hematocrit and red blood cells that are lower than normal values. Hemoglobin functions to deliver oxygen throughout the body and gives color to erythrocyte cells. In addition to hemoglobin the supporting parameters for knowing someone suffering from anemia is to look at the erythrocyte index. The purpo

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Olufemi, Akanni E., Oseni B. Sola, Bamisaye E. Oluwaseyi, Raji A. Ajani, Mewoyeka O. Olusoji, and Hassan R. Olubunmi. "Hemoglobin F level in different hemoglobin variants." Korean Journal of Hematology 46, no. 2 (2011): 118. http://dx.doi.org/10.5045/kjh.2011.46.2.118.

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Rees, D. C. "Hemoglobin F and Hemoglobin E/β-Thalassemia". Journal of Pediatric Hematology/Oncology 22, № 6 (2000): 567–72. http://dx.doi.org/10.1097/00043426-200011000-00025.

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Fuentes-Arderiu, X. ""Glycohemoglobin," not "glycated hemoglobin" or "glycosylated hemoglobin"." Clinical Chemistry 36, no. 6 (1990): 1254. http://dx.doi.org/10.1093/clinchem/36.6.1254.

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Cahit, BAĞCI. "SAGLIKLI BUZAGILARDA HEMOGLOBİN VE FÖTAL HEMOGLOBİN DÜZEYLERİ'." Ankara Üniversitesi Veteriner Fakültesi Dergisi 40, no. 1 (1993): 1. http://dx.doi.org/10.1501/vetfak_0000001695.

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Grossman, David M. "Fetal Hemoglobin and the Glycosylated Hemoglobin Assay." Annals of Internal Medicine 120, no. 6 (1994): 524. http://dx.doi.org/10.7326/0003-4819-120-6-199403150-00022.

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Alsoutary, Khalil, Frankie W. Richards, Virgil F. Fairbanks, Daniel J. McCormick, and Juraj Osterman. "Spuriously Elevated Hemoglobin A1c in a Diabetic Patient with Two Rare Hemoglobin Variants (Hemoglobin Raleigh and Hemoglobin Russ)." Endocrinologist 8, no. 2 (1998): 101–4. http://dx.doi.org/10.1097/00019616-199803000-00009.

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Nakai, Kunihiko, Toshio Ohta, Ichiro Sakuma, et al. "Inhibition of Endothelium-Dependent Relaxation by Hemoglobin in Rabbit Aortic Strips: Comparison Between Acellular Hemoglobin Derivatives and Cellular Hemoglobins." Journal of Cardiovascular Pharmacology 28, no. 1 (1996): 115–23. http://dx.doi.org/10.1097/00005344-199607000-00018.

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Khoirin, Wahyu Anita, and Rodhi Hartono. "Hemoglobin Levels in Type 2 Diabetes Mellitus Patients." Jaringan Laboratorium Medis 3, no. 1 (2021): 24–29. http://dx.doi.org/10.31983/jlm.v3i1.7918.

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Type 2 diabetes mellitus with chronic hyperglycemia can cause a hypoxic environment in the renal interstitium and can cause kidney disorders (diabetic nephropathy), this can lead to decreased kidney function and the production of erythropoietin produced by peritubular fibroblasts is disrupted, and hemoglobin is not formed optimally and occurs anemia. Thei purposei ofi thisi studyi wasi toi determinei hemoglobini levelsi in patients withi typei 2i diabetesi mellitusi in RSUD. K.R.M.T Wongsonegoro Semarang. This is a descriptive quantitative study, the data comes from the medical records of pati

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Cabrales, Pedro, Nirmala Devi Kanika, Belur N. Manjula, Amy G. Tsai, Seetharama A. Acharya та Marcos Intaglietta. "Microvascular Po2 during extreme hemodilution with hemoglobin site specifically PEGylated at Cys-93(β) in hamster window chamber". American Journal of Physiology-Heart and Circulatory Physiology 287, № 4 (2004): H1609—H1617. http://dx.doi.org/10.1152/ajpheart.00146.2004.

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The oxygen transport capacity of nonhypertensive polyethylene glycol (PEG)-conjugated hemoglobin solutions were investigated in the hamster chamber window model. Microvascular measurements were made to determine oxygen delivery in conditions of extreme hemodilution [hematocrit (Hct) 11%]. Two isovolemic hemodilution steps were performed with a 6% Dextran 70 (70-kDa molecular mass) plasma expander until Hct was 35% of control. Isovolemic blood volume exchange was continued using two surface-modified PEGylated hemoglobins (P5K2, P50 = 8.6, and P10K2, P50 = 8.3; P50 is the hemoglobin Po2 correspo

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Diniz, Laura Cristina Lima, and Pedro Ismael da Silva Junior. "Hemoglobin Reassembly of Antimicrobial Fragments from the Midgut of Triatoma infestans." Biomolecules 10, no. 2 (2020): 261. http://dx.doi.org/10.3390/biom10020261.

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Hemoglobin is one of the most important molecules of the human body. Beyond its physiological activity, hemoglobins are able to inhibit the growth of several microorganisms. Since 1999, studies have reported that antimicrobial peptides can be produced by blood-feeding insects through hemoglobin digestion, and it has been reported that Triatoma infestans can generate an antimicrobial fragment from human fibrinopeptide. Thus T. infestans intestinal content was analyzed through Reverse Phase High-Performance Liquid Chromatography (RP-HPLC), the eluted fractions were tested against Micrococcus lut

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Rutherford-Parker, Nicola J., Sean T. Campbell, Jennifer M. Colby, and Zahra Shajani-Yi. "Voxelotor Treatment Interferes With Quantitative and Qualitative Hemoglobin Variant Analysis in Multiple Sickle Cell Disease Genotypes." American Journal of Clinical Pathology 154, no. 5 (2020): 627–34. http://dx.doi.org/10.1093/ajcp/aqaa067.

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Abstract Objectives Voxelotor was recently approved for use in the United States as a treatment for sickle cell disease (SCD) and has been shown to interfere with the quantitation of hemoglobin (Hb) S percentage. This study aimed to determine the effect of voxelotor on the quantitation of hemoglobin variant levels in patients with multiple SCD genotypes. Methods In vitro experiments were performed to assess the impact of voxelotor treatment on hemoglobin variant testing. Whole blood samples were incubated with voxelotor and then analyzed by routinely used quantitative and qualitative clinical

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Priest, John R., Jan Watterson, Richard T. Jones, Anne E. Faassen, and Bo E. Hedlund. "Mutant Fetal Hemoglobin Causing Cyanosis in a Newborn." Pediatrics 83, no. 5 (1989): 734–36. http://dx.doi.org/10.1542/peds.83.5.734.

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A well but cyanotic newborn was found to have a mutant γ-globin chain, leading to a functionally abnormal fetal hemoglobin. A single amino acid substitution was found in a site consistent with known adult M hemoglobins. This patient showed no clinical evidence of cyanosis at 5 weeks of age as γ-chain synthesis was replaced by β-chain synthesis. A sibling born 20 months later was also cyanotic and the same mutant hemoglobin was found.

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