| D007532 |
Isoleucine |
An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels. |
Alloisoleucine,Isoleucine, L-Isomer,L-Isoleucine,Isoleucine, L Isomer,L-Isomer Isoleucine |
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| D007930 |
Leucine |
An essential branched-chain amino acid important for hemoglobin formation. |
L-Leucine,Leucine, L-Isomer,L-Isomer Leucine,Leucine, L Isomer |
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| D010434 |
Pepsin A |
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice. |
Pepsin,Pepsin 1,Pepsin 3 |
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| D010435 |
Pepsinogens |
Proenzymes secreted by chief cells, mucous neck cells, and pyloric gland cells, which are converted into pepsin in the presence of gastric acid or pepsin itself. (Dorland, 28th ed) In humans there are 2 related pepsinogen systems: PEPSINOGEN A (formerly pepsinogen I or pepsinogen) and PEPSINOGEN C (formerly pepsinogen II or progastricsin). Pepsinogen B is the name of a pepsinogen from pigs. |
Pepsinogen B |
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| D010443 |
Peptide Chain Termination, Translational |
A process of GENETIC TRANSLATION whereby the terminal amino acid is added to a lengthening polypeptide. This termination process is signaled from the MESSENGER RNA, by one of three termination codons (CODON, TERMINATOR) that immediately follows the last amino acid-specifying CODON. |
Chain Termination, Peptide, Translational,Protein Biosynthesis Termination,Protein Chain Termination, Translational,Protein Translation Termination,Translation Termination, Genetic,Translation Termination, Protein,Translational Peptide Chain Termination,Translational Termination, Protein,Biosynthesis Termination, Protein,Genetic Translation Termination,Protein Translational Termination,Termination, Genetic Translation,Termination, Protein Biosynthesis,Termination, Protein Translation,Termination, Protein Translational |
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| D002848 |
Chromatography, DEAE-Cellulose |
A type of ion exchange chromatography using diethylaminoethyl cellulose (DEAE-CELLULOSE) as a positively charged resin. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) |
DEAE-Cellulose Chromatography,Chromatography, DEAE Cellulose,DEAE Cellulose Chromatography |
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| D004789 |
Enzyme Activation |
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. |
Activation, Enzyme,Activations, Enzyme,Enzyme Activations |
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| D006868 |
Hydrolysis |
The process of cleaving a chemical compound by the addition of a molecule of water. |
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| D000595 |
Amino Acid Sequence |
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. |
Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein |
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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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