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The adaptation of polar fishes to climatic changes: Structure, function and phylogeny of haemoglobin.

https://arctichealth.org/en/permalink/ahliterature86911
Source
IUBMB Life. 2008 Jan;60(1):29-40
Publication Type
Article
Date
Jan-2008
Author
Verde Cinzia
Giordano Daniela
di Prisco Guido
Author Affiliation
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, Naples, Italy.
Source
IUBMB Life. 2008 Jan;60(1):29-40
Date
Jan-2008
Language
English
Publication Type
Article
Keywords
Adaptation, Physiological
Animals
Antarctic Regions
Antifreeze Proteins - genetics
Arctic Regions
Cold Climate
Evolution, Molecular
Fishes - physiology
Hemoglobins - chemistry - genetics - physiology
Oxygen - blood
Phylogeny
Abstract
In the Antarctic, fishes of dominant suborder Notothenioidei have evolved in a unique thermal scenario. Phylogenetically related taxa of the suborder live in a wide range of latitudes, in Antarctic, sub-Antarctic and temperate oceans. Consequently, they offer a remarkable opportunity to study the physiological and biochemical characters gained and, conversely, lost during their evolutionary history. The evolutionary perspective has also been pursued by comparative studies of some features of the heme protein devoted to O(2) transport in fish living in the other polar region, the Arctic. The two polar regions differ by age and isolation. Fish living in each habitat have undergone regional constraints and fit into different evolutionary histories. The aim of this contribution is to survey the current knowledge of molecular structure, functional features, phylogeny and adaptations of the haemoglobins of fish thriving in the Antarctic, sub-Antarctic and Arctic regions (with some excursions in the temperate latitudes), in search of insights into the convergent processes evolved in response to cooling. Current climate change may disturb adaptation, calling for strategies aimed at neutralising threats to biodiversity.
PubMed ID
18379990 View in PubMed
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A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans.

https://arctichealth.org/en/permalink/ahliterature132571
Source
Biochemistry. 2011 Aug 30;50(34):7350-60
Publication Type
Article
Date
Aug-30-2011
Author
Yue Yuan
Tong-Jian Shen
Priyamvada Gupta
Nancy T Ho
Virgil Simplaceanu
Tsuey Chyi S Tam
Michael Hofreiter
Alan Cooper
Kevin L Campbell
Chien Ho
Author Affiliation
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States.
Source
Biochemistry. 2011 Aug 30;50(34):7350-60
Date
Aug-30-2011
Language
English
Publication Type
Article
Keywords
Alkanesulfonic Acids - chemistry
Amino Acid Sequence
Animals
Biophysical Processes
Blood Substitutes - metabolism
Buffers
Elephants
Hemoglobin A2 - chemistry - metabolism
Hemoglobins - chemistry - metabolism
Humans
Hydrogen-Ion Concentration
Mammoths
Molecular Sequence Data
Morpholines - chemistry
Oxygen - metabolism
Phosphates - chemistry
Temperature
Abstract
This study is aimed at investigating the molecular basis of environmental adaptation of woolly mammoth hemoglobin (Hb) to the harsh thermal conditions of the Pleistocene ice ages. To this end, we have carried out a comparative biochemical-biophysical characterization of the structural and functional properties of recombinant hemoglobins (rHb) from woolly mammoth (rHb WM) and Asian elephant (rHb AE) in relation to human hemoglobins Hb A and Hb A(2) (a minor component of human blood). We have obtained oxygen equilibrium curves and calculated O(2) affinities, Bohr effects, and the apparent heat of oxygenation (?H) in the presence and absence of allosteric effectors [inorganic phosphate and inositol hexaphosphate (IHP)]. Here, we show that the four Hbs exhibit distinct structural properties and respond differently to allosteric effectors. In addition, the apparent heat of oxygenation (?H) for rHb WM is less negative than that of rHb AE, especially in phosphate buffer and the presence of IHP, suggesting that the oxygen affinity of mammoth blood was also less sensitive to temperature change. Finally, (1)H NMR spectroscopy data indicates that both a(1)(ß/d)(1) and a(1)(ß/d)(2) interfaces in rHb WM and rHb AE are perturbed, whereas only the a(1)d(1) interface in Hb A(2) is perturbed compared to that in Hb A. The distinct structural and functional features of rHb WM presumably facilitated woolly mammoth survival in the Arctic environment.
Notes
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PubMed ID
21806075 View in PubMed
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Dietary acrylamide intake during pregnancy and fetal growth-results from the Norwegian mother and child cohort study (MoBa).

https://arctichealth.org/en/permalink/ahliterature118477
Source
Environ Health Perspect. 2013 Mar;121(3):374-9
Publication Type
Article
Date
Mar-2013
Author
Talita Duarte-Salles
Hans von Stedingk
Berit Granum
Kristine B Gützkow
Per Rydberg
Margareta Törnqvist
Michelle A Mendez
Gunnar Brunborg
Anne Lise Brantsæter
Helle Margrete Meltzer
Jan Alexander
Margaretha Haugen
Author Affiliation
Division of Environmental Medicine, Norwegian Institute of Public Health, Oslo, Norway.
Source
Environ Health Perspect. 2013 Mar;121(3):374-9
Date
Mar-2013
Language
English
Publication Type
Article
Keywords
Acrylamide - administration & dosage - pharmacology
Cohort Studies
Diet
Environmental Exposure
Female
Fetal Development - drug effects
Hemoglobins - chemistry
Humans
Norway
Pregnancy
Questionnaires
Abstract
Acrylamide has shown developmental and reproductive toxicity in animals, as well as neurotoxic effects in humans with occupational exposures. Because it is widespread in food and can pass through the human placenta, concerns have been raised about potential developmental effects of dietary exposures in humans.
We assessed associations of prenatal exposure to dietary acrylamide with small for gestational age (SGA) and birth weight.
This study included 50,651 women in the Norwegian Mother and Child Cohort Study (MoBa). Acrylamide exposure assessment was based on intake estimates obtained from a food frequency questionnaire (FFQ), which were compared with hemoglobin (Hb) adduct measurements reflecting acrylamide exposure in a subset of samples (n = 79). Data on infant birth weight and gestational age were obtained from the Medical Birth Registry of Norway. Multivariable regression was used to estimate associations between prenatal acrylamide and birth outcomes.
Acrylamide intake during pregnancy was negatively associated with fetal growth. When women in the highest quartile of acrylamide intake were compared with women in the lowest quartile, the multivariable-adjusted odds ratio (OR) for SGA was 1.11 (95% CI: 1.02, 1.21) and the coefficient for birth weight was -25.7 g (95% CI: -35.9, -15.4). Results were similar after excluding mothers who smoked during pregnancy. Maternal acrylamide- and glycidamide-Hb adduct levels were correlated with estimated dietary acrylamide intakes (Spearman correlations = 0.24; 95% CI: 0.02, 0.44; and 0.48; 95% CI: 0.29, 0.63, respectively).
Lowering dietary acrylamide intake during pregnancy may improve fetal growth.
Notes
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PubMed ID
23204292 View in PubMed
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Dietary determinants for Hb-acrylamide and Hb-glycidamide adducts in Danish non-smoking women.

https://arctichealth.org/en/permalink/ahliterature101882
Source
Br J Nutr. 2011 May;105(9):1381-7
Publication Type
Article
Date
May-2011
Author
Outzen M
Egeberg R
Dragsted L
Christensen J
Olesen PT
Frandsen H
Overvad K
Anne Tjønneland A
Olsen A
Author Affiliation
Department of Diet, Cancer and Health, Institute of Cancer Epidemiology, Danish Cancer Society, Strandboulevarden 49, Copenhagen, Denmark. outzen@cancer.dk
Source
Br J Nutr. 2011 May;105(9):1381-7
Date
May-2011
Language
English
Publication Type
Article
Keywords
Acrylamide - chemistry - metabolism
Case-Control Studies
Denmark
Diet
Epoxy Compounds - chemistry - metabolism
Female
Food Habits
Hemoglobins - chemistry - metabolism
Humans
Middle Aged
Postmenopause
Risk factors
Abstract
Acrylamide (AA) is a probable human carcinogen that is formed in heat-treated carbohydrate-rich foods. The validity of FFQ to assess AA exposure has been questioned. The aim of the present cross-sectional study was to investigate dietary determinants of Hb-AA and Hb-glycidamide (GA) adducts. The study included 537 non-smoking women aged 50-65 years who participated in the Diet, Cancer and Health cohort (1993-97). At study baseline, blood samples and information on dietary and lifestyle variables obtained from self-administered questionnaires were collected. From blood samples, Hb-AA and Hb-GA in erythrocytes were analysed by liquid chromatography/MS/MS. Dietary determinants were evaluated by multiple linear regression analyses adjusted for age and smoking behaviour among ex-smokers. The median for Hb-AA was 35 pmol/g globin (5th percentile 17, 95th percentile 89) and for Hb-GA 21 pmol/g globin (5th percentile 8, 95th percentile 49). Of the dietary factors studied, intakes of coffee and chips were statistically significantly associated with a 4 % per 200 g/d (95 % CI 2, 7; P 
PubMed ID
21272397 View in PubMed
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Effects on the peripheral nervous system of tunnel workers exposed to acrylamide and N-methylolacrylamide.

https://arctichealth.org/en/permalink/ahliterature67258
Source
Scand J Work Environ Health. 2004 Feb;30(1):21-9
Publication Type
Article
Date
Feb-2004
Author
Helge Kjuus
Lars Ole Goffeng
Mona Skard Heier
Hans Sjöholm
Steinar Ovrebø
Vidar Skaug
Birgit Paulsson
Margareta Törnqvist
Stein Brudal
Author Affiliation
Department of Occupational Medicine, National Institute of Occupational Health, Oslo, Norway. Helge.Kjuus@stami.no
Source
Scand J Work Environ Health. 2004 Feb;30(1):21-9
Date
Feb-2004
Language
English
Publication Type
Article
Keywords
Acrylamide - blood - toxicity
Acrylamides - blood - toxicity
Adult
Comparative Study
Construction Materials - toxicity
Follow-Up Studies
Hemoglobins - chemistry
Humans
Middle Aged
Neural Conduction - drug effects - physiology
Occupational Exposure - adverse effects - analysis
Occupational Health
Paresthesia - chemically induced - physiopathology
Peripheral Nervous System - drug effects - physiopathology
Railroads - manpower
Research Support, Non-U.S. Gov't
Smoking
Sweden
Abstract
OBJECTIVES: This study evaluates the possible toxic effects on the peripheral nervous system of tunnel workers exposed to acrylamide and N-methylolacrylamide during grouting work. METHODS: Symptoms and nerve conduction velocities (NCV) were recorded for 24 tunnel workers 4 and 16 months after the cessation of exposure during grouting operations. Fifty tunnel workers not involved in grouting operations served as referents. Exposure was assessed by questionnaires, qualitative exposure indices, and measurements of hemoglobin adducts after the cessation of exposure. RESULTS:The exposed workers reported a higher prevalence of symptoms during grouting work than they did in an examination 16 months later. A statistically significant reduction in the mean sensory NCV of the ulnar nerve was observed 4 months postexposure when compared with the values of the reference group (52.3 versus 58.9 m/s, P = 0.001), and the mean ulnar distal delay was prolonged (3.1 versus 2.5 ms, P = 0.001). Both measures were significantly improved when measured 1 year later. Exposure-related improvements were observed from 4 to 16 months postexposure for both the median (motor and sensory NCV and F-response) and ulnar (sensory NCV, F-response) nerves. A significant reversible reduction in the mean sensory amplitude of the median nerve was also observed, while the mean sensory amplitude of the sural nerve was significantly reduced after 16 months. CONCLUSIONS: The results indicate demyelinating and axonal changes in peripheral nerves of tunnel workers in relation to exposure to N-methylolacrylamide and acrylamide during grouting operations. The changes were slight, mostly subclinical, and most of the effects were reversible, with normalization after 1 year.
Notes
Comment In: Scand J Work Environ Health. 2004 Jun;30(3):253; author reply 253-415250655
PubMed ID
15018025 View in PubMed
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From the Arctic to fetal life: physiological importance and structural basis of an 'additional' chloride-binding site in haemoglobin.

https://arctichealth.org/en/permalink/ahliterature181409
Source
Biochem J. 2004 Jun 15;380(Pt 3):889-96
Publication Type
Article
Date
Jun-15-2004
Author
M Cristina De Rosa
Massimo Castagnola
Claudia Bertonati
Antonio Galtieri
Bruno Giardina
Author Affiliation
Institute of Biochemistry and Clinical Biochemistry and CNR Institute of Chemistry of Molecular Recognition, Catholic University of Rome, L.go F. Vito 1, 00168 Rome, Italy.
Source
Biochem J. 2004 Jun 15;380(Pt 3):889-96
Date
Jun-15-2004
Language
English
Publication Type
Article
Keywords
2,3-Diphosphoglycerate - metabolism
Adult
Amino Acids - metabolism - physiology
Animals
Binding Sites - physiology
Cattle - blood
Chlorides - metabolism - physiology
Computational Biology - methods
Computer simulation
Erythrocytes - chemistry
Fetal Hemoglobin - chemistry - physiology
Fetus - blood supply
Hemoglobins - chemistry - physiology
Horses - blood
Humans
Oxygen - metabolism
Reindeer - blood
Species Specificity
Swine - blood
Thermodynamics
Ursidae - blood
Abstract
Haemoglobins from mammals of sub-Arctic and Arctic species, as well as fetal human Hb, are all characterized by a significantly lower Delta H of oxygenation compared with the majority of mammalian haemoglobins from temperate species (exceptions are represented by some cold-resistant species, such as cow, horse and pig). This has been interpreted as an adaptive mechanism of great importance from a physiological point of view. To date, the molecular basis of this thermodynamic characteristic is still not known. In the present study, we show that binding of extra chloride (with respect to adult human Hb) ions to Hb would significantly contribute to lowering the overall heat of oxygenation, thus providing a molecular basis for the low effect of temperature on the oxygenation-deoxygenation cycle. To this aim, the oxygen binding properties of bovine Hb, bear (Ursus arctos) Hb and horse Hb, which are representative of this series of haemoglobins, have been studied with special regard to the effect of heterotropic ligands, such as organic phosphates (namely 2,3-diphosphoglycerate) and chloride. Functional results are consistent with a mechanism for ligand binding that involves an additional binding site for chloride ion. Analysis of computational chemistry results, obtained by the GRID program, further confirm the hypothesis that the reason for the lower Delta H of oxygenation is mainly due to an increase in the number of the oxygen-linked chloride-binding sites.
Notes
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PubMed ID
14979874 View in PubMed
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The functionally distinct hemoglobins of the Arctic spotted wolffish Anarhichas minor.

https://arctichealth.org/en/permalink/ahliterature9935
Source
J Biol Chem. 2002 Sep 27;277(39):36312-20
Publication Type
Article
Date
Sep-27-2002
Author
Cinzia Verde
Vito Carratore
Antonio Riccio
Maurizio Tamburrini
Elio Parisi
Guido Di Prisco
Author Affiliation
Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via Marconi 12, I-80125 Naples, Italy.
Source
J Biol Chem. 2002 Sep 27;277(39):36312-20
Date
Sep-27-2002
Language
English
Publication Type
Article
Keywords
Adenosine Triphosphate - metabolism
Amino Acid Sequence
Animals
Binding Sites
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Cysteine - chemistry
Gene Expression Regulation
Hemoglobins - chemistry - metabolism
Hydrogen-Ion Concentration
Models, Molecular
Molecular Sequence Data
Mutation
Organophosphorus Compounds - metabolism
Oxygen - metabolism
Perciformes - metabolism
Phylogeny
Phytic Acid - metabolism
Promoter Regions (Genetics)
Protein Binding
Protein Structure, Tertiary
Research Support, Non-U.S. Gov't
Spectrum Analysis, Mass
Temperature
Time Factors
Abstract
The Arctic fish Anarhichas minor, a benthic sedentary species, displays high hemoglobin multiplicity. The three major hemoglobins (Hb 1, Hb 2, and Hb 3) show important functional differences in pH and organophosphate regulation, subunit cooperativity, and response of oxygen binding to temperature. Hb 1 and Hb 2 display a low, effector-enhanced Bohr effect and no Root effect. In contrast, Hb 3 displays pronounced Bohr and Root effects, accompanied by strong organophosphate regulation. Hb 1 has the beta (beta(1)) chain in common with Hb 2; Hb 3 and Hb 2 share the alpha (alpha(2)) chain. The amino acid sequences have been established. Several substitutions in crucial positions were observed, such as Cys in place of C-terminal His in the beta(1) chain of Hb 1 and Hb 2. In Hb 3, Val E11 of the beta(2) chain is replaced by Ile. Homology modeling revealed an unusual structure of the Hb 3 binding site of inositol hexakisphoshate. Phylogenetic analysis indicated that only Hb 2 displays higher overall similarity with the major Antarctic hemoglobins. The oxygen transport system of A. minor differs remarkably from those of Antarctic Notothenioidei, indicating distinct evolutionary pathways in the regulatory mechanisms of the fish respiratory system in the two polar environments.
PubMed ID
12118003 View in PubMed
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Health effects of occupational exposure to acrylamide using hemoglobin adducts as biomarkers of internal dose.

https://arctichealth.org/en/permalink/ahliterature193241
Source
Scand J Work Environ Health. 2001 Aug;27(4):219-26
Publication Type
Article
Date
Aug-2001
Author
L. Hagmar
M. Törnqvist
C. Nordander
I. Rosén
M. Bruze
A. Kautiainen
A L Magnusson
B. Malmberg
P. Aprea
F. Granath
A. Axmon
Author Affiliation
Department of Occupational and Environmental Medicine, University Hospital, Lund, Sweden. lars.hagmar@ymed.lu.se
Source
Scand J Work Environ Health. 2001 Aug;27(4):219-26
Date
Aug-2001
Language
English
Publication Type
Article
Keywords
Acrylamide - adverse effects - chemistry
Biological Markers
Dermatitis, Allergic Contact - etiology
Dose-Response Relationship, Drug
Engineering
Hemoglobins - chemistry
Humans
Occupational Exposure
Peripheral Nervous System - drug effects - physiopathology
Questionnaires
Sweden
Abstract
This study assessed the health effects of occupational acrylamide exposure using hemoglobin (Hb) adducts as biomarkers of internal dose.
Two hundred and ten tunnel workers exposed for about 2 months to a chemical-grouting agent containing acrylamide and N-methylolacrylamide underwent a health examination. Blood samples were drawn for the analysis of Hb adducts of acrylamide. Fifty workers claiming recently developed or deteriorated symptoms of the peripheral nervous system (PNS) were referred to a neurophysiological examination. Workers with Hb-adduct levels exceeding 0.3 nmol/g globin attended follow-up examinations 6, 12, and 18 months after exposure cessation.
Forty-seven workers had Hb-adduct levels within the normal background range (0.02-0.07 nmol/g globin), while the remaining 163 had increased levels up to a maximum of 17.7 nmol/g globin. Clear-cut dose-response associations were found between the Hb-adduct levels and PNS symptoms. Thirty-nine percent of those with Hb-adduct levels exceeding 1 nmol/g globin experienced tingling or numbness in their hands or feet. A no-observed adverse effect level of 0.51 nmol/g globin was estimated for numbness or tingling in the feet or legs. For 23 workers there was strong evidence of PNS impairment due to occupational exposure to acrylamide. All but two had recovered 18 months after the cessation of exposure.
Occupational exposure to a grouting agent containing acrylamide resulted in PNS symptoms and signs. The use of Hb adducts of acrylamide as a biomarker of internal dose revealed strong dose-response associations. The PNS symptoms were, however, generally mild, and in almost all cases they were reversible.
Notes
Comment In: Scand J Work Environ Health. 2001 Aug;27(4):217-811560334
PubMed ID
11560335 View in PubMed
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Polymerization of hemoglobins in Arctic fish: Lycodes reticulatus and Gadus morhua.

https://arctichealth.org/en/permalink/ahliterature135302
Source
IUBMB Life. 2011 May;63(5):346-54
Publication Type
Article
Date
May-2011
Author
Alessia Riccio
Gaetano Mangiapia
Daniela Giordano
Angela Flagiello
Roberta Tedesco
Stefano Bruno
Alessandro Vergara
Lelio Mazzarella
Guido di Prisco
Piero Pucci
Luigi Paduano
Cinzia Verde
Author Affiliation
Institute of Protein Biochemistry, CNR, Naples, Italy.
Source
IUBMB Life. 2011 May;63(5):346-54
Date
May-2011
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence
Animals
Arctic Regions
Gadus morhua
Hemoglobins - chemistry - genetics - metabolism
Humans
Molecular Sequence Data
Oxygen - metabolism
Polymerization
Protein Conformation
Sequence Alignment
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Abstract
In vitro, and possibly in vivo, hemoglobin polymerization and red blood cell sickling appear to be widespread in codfish. In this article, we show that the hemoglobins of the two Arctic fish Lycodes reticulatus and Gadus morhua also have the tendency to polymerize, as monitored by dynamic light scattering experiments. The elucidation of the primary structure of the single hemoglobin of the zoarcid L. reticulatus shows the presence of a large number of cysteyl residues in a and ß chains. Their role in eliciting the ability to produce polymers was also addressed by MALDI-TOF and TOF-TOF mass spectrometry. The G.morhua globins are also rich in Cys, but unlike in L. reticulatus, polymerization does not seem to be disulfide driven. The widespread occurrence of the polymerization phenomenon displayed by hemoglobins of Arctic fish supports the hypothesis that this feature may bea response to stressful environmental conditions.
PubMed ID
21491556 View in PubMed
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Purification of hemoglobin by ion exchange chromatography in flow-through mode with PEG as an escort.

https://arctichealth.org/en/permalink/ahliterature9436
Source
Artif Cells Blood Substit Immobil Biotechnol. 2004 May;32(2):209-27
Publication Type
Article
Date
May-2004
Author
Xiuling Lu
Dongxu Zhao
Zhiguo Su
Author Affiliation
National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China.
Source
Artif Cells Blood Substit Immobil Biotechnol. 2004 May;32(2):209-27
Date
May-2004
Language
English
Publication Type
Article
Keywords
Animals
Blood Preservation
Carbohydrates - chemistry
Cattle
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange - methods
Electrophoresis, Polyacrylamide Gel
Erythrocytes - chemistry
Freeze Drying
Hemoglobins - chemistry - isolation & purification
Hydrogen-Ion Concentration
Oxygen consumption
Polyethylene Glycols - chemistry
Research Support, Non-U.S. Gov't
Abstract
Development of hemoglobin-based blood substitutes requires production of highly purified hemoglobin. Process of hemoglobin purification by ion exchange chromatography in flow-through mode was researched and optimized. Three kinds of media including, QMA Spherosil LS (Biosepra, France) and Q Sepharose Big Beads (Amersham Bioscience, Sweden), and an anion exchange membrane column, Mustang Q (PALL, USA) were investigated and compared. Adding polyethylene glycol (PEG) as an escort in ion exchange chromatography improved the purity and recovery, and the recovery in the chromatography was increased from 75 to 95%. The mechanism of PEG effects on chromatography was discussed. The optimal chromatography step, in combination with hypotonic dilution hemolyzing and membrane separation, formed an integrated hemoglobin purification process. The total recovery in the process was 87.6%. The activity of hemoglobin was well preserved: P50 23.2 mmHg, and Hill coefficient 2.31. The product appeared as a single band in SDS-PAGE, and GF-HPLC showed only one peak. The purity of the prepared hemoglobin was more than 99.9%. The optimized process is time saving and suitable for large-scale preparation of hemoglobin to provide materials for further preparation of blood substitutes.
PubMed ID
15274429 View in PubMed
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