| D007515 |
Islets of Langerhans |
Irregular microscopic structures consisting of cords of endocrine cells that are scattered throughout the PANCREAS among the exocrine acini. Each islet is surrounded by connective tissue fibers and penetrated by a network of capillaries. There are four major cell types. The most abundant beta cells (50-80%) secrete INSULIN. Alpha cells (5-20%) secrete GLUCAGON. PP cells (10-35%) secrete PANCREATIC POLYPEPTIDE. Delta cells (~5%) secrete SOMATOSTATIN. |
Islands of Langerhans,Islet Cells,Nesidioblasts,Pancreas, Endocrine,Pancreatic Islets,Cell, Islet,Cells, Islet,Endocrine Pancreas,Islet Cell,Islet, Pancreatic,Islets, Pancreatic,Langerhans Islands,Langerhans Islets,Nesidioblast,Pancreatic Islet |
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| D007700 |
Kinetics |
The rate dynamics in chemical or physical systems. |
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| 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 |
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| D010447 |
Peptide Hydrolases |
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. |
Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide |
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| D011490 |
Protein Disulfide Reductase (Glutathione) |
An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2. |
Glutathione Insulin Transhydrogenase,Glutathione Protein Disulfide Oxidoreductase,Thiol-Disulfide Oxidoreductase,Thiol-Protein Disulfide Oxidoreductase,Disulfide Oxidoreductase, Thiol-Protein,Insulin Transhydrogenase, Glutathione,Oxidoreductase, Thiol-Disulfide,Oxidoreductase, Thiol-Protein Disulfide,Thiol Disulfide Oxidoreductase,Thiol Protein Disulfide Oxidoreductase,Transhydrogenase, Glutathione Insulin |
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| D002268 |
Carboxypeptidases |
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue. |
Carboxypeptidase |
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| 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 |
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| D013347 |
Subcellular Fractions |
Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163) |
Fraction, Subcellular,Fractions, Subcellular,Subcellular Fraction |
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| D013379 |
Substrate Specificity |
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. |
Specificities, Substrate,Specificity, Substrate,Substrate Specificities |
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| D014357 |
Trypsin |
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. |
Tripcellim,Trypure,beta-Trypsin,beta Trypsin |
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