Characteristics of hexokinase, pyruvate kinase, and glucose‐6‐phosphate dehydrogenase during adult and neonatal reticulocyte maturation

Erythrocytes from adults and newborn infants (at term and premature) were separated by Percoll density gradient centrifugation into four fractions of increasing density. Glycolytic enzymes, especially the age‐dependent ones, hexokinase (EC 2.7.1.1, HK), pyruvate kinase (EC 2.7.1.40, PK), and glucose...

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Veröffentlicht in:American journal of hematology 1985-11, Vol.20 (3), p.203-215
Hauptverfasser: Jansen, G., Koenderman, L., Rijksen, G., Cats, B. P., Staal, G. E. J.
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container_end_page 215
container_issue 3
container_start_page 203
container_title American journal of hematology
container_volume 20
creator Jansen, G.
Koenderman, L.
Rijksen, G.
Cats, B. P.
Staal, G. E. J.
description Erythrocytes from adults and newborn infants (at term and premature) were separated by Percoll density gradient centrifugation into four fractions of increasing density. Glycolytic enzymes, especially the age‐dependent ones, hexokinase (EC 2.7.1.1, HK), pyruvate kinase (EC 2.7.1.40, PK), and glucose‐6‐phosphate dehydrogenase (EC 1.1.1.49, G6PD) were studied during reticulocyte maturation and further red cell senescence. Analysis of the fraction with lowest density showed an almost linear and steep decline of HK, PK, and G6PD activity with a decreasing number of reticulocytes. In the next three fractions of increasing density, the activity decline was far less. These data are therefore illustrative for a biphasic activity decay pattern of HK, PK, and G6PD during both adult and neonatal red cell aging. The strong decline in HK activity could not be ascribed to the disappearance of a particulate (mitochondrial) bound fraction of the enzyme during reticulocyte maturation. All hexokinase activity in human reticulocytes was found to be cytosolic in contrast with rabbit reticulocytes in which 70% of HK activity was particulate.
doi_str_mv 10.1002/ajh.2830200302
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The strong decline in HK activity could not be ascribed to the disappearance of a particulate (mitochondrial) bound fraction of the enzyme during reticulocyte maturation. All hexokinase activity in human reticulocytes was found to be cytosolic in contrast with rabbit reticulocytes in which 70% of HK activity was particulate.</description><identifier>ISSN: 0361-8609</identifier><identifier>EISSN: 1096-8652</identifier><identifier>DOI: 10.1002/ajh.2830200302</identifier><identifier>PMID: 4061449</identifier><identifier>CODEN: AJHEDD</identifier><language>eng</language><publisher>New York: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Adult ; Animals ; Biological and medical sciences ; Cell Compartmentation ; Cell Separation ; Electrophoresis, Cellulose Acetate ; Erythrocyte Aging ; Erythrocytes - enzymology ; Fundamental and applied biological sciences. 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P.</creatorcontrib><creatorcontrib>Staal, G. E. J.</creatorcontrib><title>Characteristics of hexokinase, pyruvate kinase, and glucose‐6‐phosphate dehydrogenase during adult and neonatal reticulocyte maturation</title><title>American journal of hematology</title><addtitle>Am J Hematol</addtitle><description>Erythrocytes from adults and newborn infants (at term and premature) were separated by Percoll density gradient centrifugation into four fractions of increasing density. Glycolytic enzymes, especially the age‐dependent ones, hexokinase (EC 2.7.1.1, HK), pyruvate kinase (EC 2.7.1.40, PK), and glucose‐6‐phosphate dehydrogenase (EC 1.1.1.49, G6PD) were studied during reticulocyte maturation and further red cell senescence. Analysis of the fraction with lowest density showed an almost linear and steep decline of HK, PK, and G6PD activity with a decreasing number of reticulocytes. In the next three fractions of increasing density, the activity decline was far less. 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Psychology</topic><topic>Glucosephosphate Dehydrogenase - blood</topic><topic>glucose‐6‐phosphate dehydrogenase</topic><topic>hexokinase</topic><topic>Hexokinase - blood</topic><topic>Humans</topic><topic>Infant, Newborn</topic><topic>Isoenzymes - blood</topic><topic>pyruvate kinase</topic><topic>Pyruvate Kinase - blood</topic><topic>Rabbits</topic><topic>Reticulocytes - enzymology</topic><topic>Reticulocytes - physiology</topic><topic>Vertebrates: blood, hematopoietic organs, reticuloendothelial system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jansen, G.</creatorcontrib><creatorcontrib>Koenderman, L.</creatorcontrib><creatorcontrib>Rijksen, G.</creatorcontrib><creatorcontrib>Cats, B. P.</creatorcontrib><creatorcontrib>Staal, G. E. 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source MEDLINE; Wiley Online Library Journals Frontfile Complete
subjects Adult
Animals
Biological and medical sciences
Cell Compartmentation
Cell Separation
Electrophoresis, Cellulose Acetate
Erythrocyte Aging
Erythrocytes - enzymology
Fundamental and applied biological sciences. Psychology
Glucosephosphate Dehydrogenase - blood
glucose‐6‐phosphate dehydrogenase
hexokinase
Hexokinase - blood
Humans
Infant, Newborn
Isoenzymes - blood
pyruvate kinase
Pyruvate Kinase - blood
Rabbits
Reticulocytes - enzymology
Reticulocytes - physiology
Vertebrates: blood, hematopoietic organs, reticuloendothelial system
title Characteristics of hexokinase, pyruvate kinase, and glucose‐6‐phosphate dehydrogenase during adult and neonatal reticulocyte maturation
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