Biomaterial Database

[Adaptation of rats following sodium-nitrite-induced methemoglobinemia]. 1975

D Pankow, and W Ponsold, and M D Liedke, and G Gessner, and A Pfordte

Adaptation of rats following sodium nitrite induced methemoglobinemia. The effect of repeated intraperitoneal injections of sodium nitrite on methemoglobin, hemoglobin and blood sugar level, on leucine aminopeptidase activity in plasma and methemoglobin reductase activity in red blood cells was investigated in rats. Repeated methemoglobinemia produced gradual disappearance of hyperglycemia, changes of hemoglobin content in blood and increase of methemoglobin reductase activity in red blood cells.

UI	MeSH Term	Description	Entries
D007931	Leucyl Aminopeptidase	A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.	Cytosol Aminopeptidase,Leucine Aminopeptidase,L-Leucylnaphthylamidase,Methoxyleucine Aminopeptidase,Peptidase S,Zinc-Manganese-Leucine Aminopeptidase,Aminopeptidase, Cytosol,Aminopeptidase, Leucine,Aminopeptidase, Leucyl,Aminopeptidase, Methoxyleucine,Aminopeptidase, Zinc-Manganese-Leucine,Zinc Manganese Leucine Aminopeptidase
D008297	Male		Males
D008708	Methemoglobinemia	The presence of methemoglobin in the blood, resulting in cyanosis. A small amount of methemoglobin is present in the blood normally, but injury or toxic agents convert a larger proportion of hemoglobin into methemoglobin, which does not function reversibly as an oxygen carrier. Methemoglobinemia may be due to a defect in the enzyme NADH methemoglobin reductase (an autosomal recessive trait) or to an abnormality in hemoglobin M (an autosomal dominant trait). (Dorland, 27th ed)	Methemoglobinemias
D009573	Nitrites	Salts of nitrous acid or compounds containing the group NO2-. The inorganic nitrites of the type MNO2 (where M	Nitrite
D001786	Blood Glucose	Glucose in blood.	Blood Sugar,Glucose, Blood,Sugar, Blood
D004912	Erythrocytes	Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.	Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D006454	Hemoglobins	The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.	Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D000222	Adaptation, Physiological	The non-genetic biological changes of an organism in response to challenges in its ENVIRONMENT.	Adaptation, Physiologic,Adaptations, Physiologic,Adaptations, Physiological,Adaptive Plasticity,Phenotypic Plasticity,Physiological Adaptation,Physiologic Adaptation,Physiologic Adaptations,Physiological Adaptations,Plasticity, Adaptive,Plasticity, Phenotypic
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D042966	Cytochrome-B(5) Reductase	A FLAVOPROTEIN oxidoreductase that occurs both as a soluble enzyme and a membrane-bound enzyme due to ALTERNATIVE SPLICING of a single mRNA. The soluble form is present mainly in ERYTHROCYTES and is involved in the reduction of METHEMOGLOBIN. The membrane-bound form of the enzyme is found primarily in the ENDOPLASMIC RETICULUM and outer mitochondrial membrane, where it participates in the desaturation of FATTY ACIDS; CHOLESTEROL biosynthesis and drug metabolism. A deficiency in the enzyme can result in METHEMOGLOBINEMIA.	Methemoglobin Reductase,NADH Cytochrome B5 Reductase,NADH Methemoglobin Reductase,NADH-Cytochrome B5 Reductase,NADH-Ferrihemoglobin Reductase,B5 Reductase, NADH-Cytochrome,Methemoglobin Reductase, NADH,NADH Ferrihemoglobin Reductase,Reductase, Methemoglobin,Reductase, NADH Methemoglobin,Reductase, NADH-Ferrihemoglobin