BIOMAT Database Logo BIOMAT Database Logo

Slide histochemistry of enzyme activity in normal and atherosclerotic canine aorta. 1968

L J Rubinstein, and N Maier, and H Haimovici

UI MeSH Term Description Entries
D007770 L-Lactate Dehydrogenase A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist. Lactate Dehydrogenase,Dehydrogenase, L-Lactate,Dehydrogenase, Lactate,L Lactate Dehydrogenase
D009243 NAD A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D009249 NADP Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed) Coenzyme II,Nicotinamide-Adenine Dinucleotide Phosphate,Triphosphopyridine Nucleotide,NADPH,Dinucleotide Phosphate, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide Phosphate,Nucleotide, Triphosphopyridine,Phosphate, Nicotinamide-Adenine Dinucleotide
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D004285 Dogs The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065) Canis familiaris,Dog
D005993 Glycerolphosphate Dehydrogenase Alpha-Glycerophosphate Dehydrogenase,Glycerol-3-Phosphate Dehydrogenase,Glycerophosphate Dehydrogenase,Glycerophosphate Oxidase,Alpha Glycerophosphate Dehydrogenase,Dehydrogenase, Alpha-Glycerophosphate,Dehydrogenase, Glycerol-3-Phosphate,Dehydrogenase, Glycerolphosphate,Dehydrogenase, Glycerophosphate,Glycerol 3 Phosphate Dehydrogenase,Oxidase, Glycerophosphate
D006019 Glycolysis A metabolic process that converts GLUCOSE into two molecules of PYRUVIC ACID through a series of enzymatic reactions. Energy generated by this process is conserved in two molecules of ATP. Glycolysis is the universal catabolic pathway for glucose, free glucose, or glucose derived from complex CARBOHYDRATES, such as GLYCOGEN and STARCH. Embden-Meyerhof Pathway,Embden-Meyerhof-Parnas Pathway,Embden Meyerhof Parnas Pathway,Embden Meyerhof Pathway,Embden-Meyerhof Pathways,Pathway, Embden-Meyerhof,Pathway, Embden-Meyerhof-Parnas,Pathways, Embden-Meyerhof
D006651 Histocytochemistry Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods. Cytochemistry
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
D001011 Aorta The main trunk of the systemic arteries. Aortas

Related Publications

L J Rubinstein, and N Maier, and H Haimovici
Sialyltransferase activity in normal and atherosclerotic human aorta intima.
April 2001, Biochemistry. Biokhimiia,
L J Rubinstein, and N Maier, and H Haimovici
Cholesterol esterase activity of normal and atherosclerotic rabbit aorta.
February 1966, Biochimica et biophysica acta,
L J Rubinstein, and N Maier, and H Haimovici
ADPase activity of normal and atherosclerotic human aorta intima.
June 1977, Thrombosis and haemostasis,
L J Rubinstein, and N Maier, and H Haimovici
Primary cultures of enzyme-isolated cells from normal and atherosclerotic human aorta.
January 1984, Medical biology,
L J Rubinstein, and N Maier, and H Haimovici
Lipoproteins in normal and atherosclerotic aorta.
August 1990, European heart journal,
L J Rubinstein, and N Maier, and H Haimovici
[ULTRASTRUCTURE OF THE NORMAL AND ATHEROSCLEROTIC AORTA].
July 1964, Archivio "de Vecchi" per l'anatomia patologica e la medicina clinica,
L J Rubinstein, and N Maier, and H Haimovici
Collagen types in normal and atherosclerotic human aorta.
January 1983, Indian heart journal,
L J Rubinstein, and N Maier, and H Haimovici
[Adiponectin in normal and atherosclerotic intima of human aorta].
January 2022, Arkhiv patologii,
L J Rubinstein, and N Maier, and H Haimovici
Canine atrioventricular node: scanning electron microscopy and enzyme histochemistry.
February 1986, American journal of veterinary research,
L J Rubinstein, and N Maier, and H Haimovici
Enzyme histochemistry of normal and neoplastic transitional epithelium.
December 1984, American journal of clinical pathology,
Copied contents to your clipboard!