| peptic | Pertaining to pepsin or to digestion, related to the action of gastric juices. Origin: Gr. Peptikos (18 Nov 1997) |
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| peptic cell | <pathology> Cells of the basal part of the gastric glands of the stomach. They contain extensive rough endoplasmic reticulum and zymogen granules and secrete pepsinogen, the inactive precursor of pepsin and rennin. (18 Nov 1997) |
| peptic digestion | That part of digestion, chiefly of the proteins, carried on in the stomach by the enzymes of the gastric juice. Synonym: peptic digestion. (05 Mar 2000) |
| peptic gland | A pepsin-secreting gland. See: gastric glands. (05 Mar 2000) |
| peptic ulcer | <gastroenterology> An ulcer in the wall of the stomach or duodenum resulting from the digestive action of the gastric juice on the mucous membrane when the latter is rendered susceptible to its action. (13 Nov 1997) |
| peptic ulcer perforation | Penetration of a peptic ulcer through the stomach wall. May be free, i.e., at a point where the stomach wall faces a real or potential space,, or confined, i.e., at a point where the stomach wall is defended by contiguous or adjacent structures, such as the pancreas. (12 Dec 1998) |
| peptichemio | <chemical> A mixture of six synthetic oligopeptides, each containing melphalan. It is used as a broad-spectrum antineoplastic due to its alkylating and antimetabolic actions but, is toxic to bone marrow, gastrointestinal system and vasculature. Pharmacological action: antimetabolites, antineoplastic, antineoplastic agent, alkylating. Chemical name: Peptichemio (12 Dec 1998) |
| peptidase | <enzyme> Alternative name for a protease. (18 Nov 1997) |
| peptidase D | <enzyme> An enzyme cleaving aminoacyl-l-proline bonds in dipeptides containing a C-terminal prolyl residue; a deficiency of this enzyme results in hyperimidodipeptiduria. Synonym: imidodipeptidase, peptidase D, prolidase. (05 Mar 2000) |
| peptidase P | <enzyme> A hydrolase cleaving C-terminal dipeptides from a variety of substrates, including angiotensin I, which is converted to angiotensin II and histidylleucine. An important step in the metabolism of certain vasopressor agents. It is a chloride-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. Only single dipeptides are released from angiotensin I and bradykinin because of the lack of activity on bonds involving proline. It may also have endopeptidase activity on some substrates. Registry number: EC 3.4.15.1 Synonym: carboxycathepsin, dipeptidyl carboxypeptidase, kinase II, peptidase P. (22 Sep 2002) |
| peptide | <biochemistry> A compound of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. (27 Sep 1997) |
| peptide antibiotic lactonase | <enzyme> Peptide lactone and water gives linear peptide Registry number: EC 3.1.1.- (26 Jun 1999) |
| peptide bond | The amide linkage between the carboxyl group of one amino acid and the amino group of another. The linkage does not allow free rotation and can occur in cis or trans configuration, the latter the most common in natural peptides, except for links to the amino group of proline, which are always cis. (18 Nov 1997) |
| peptide chain elongation | The process whereby an amino acid is joined through a substituted amide linkage to a chain of peptides. (12 Dec 1998) |
| peptide chain initiation | The process whereby the formation of a peptide chain is started. This process requires (1) the 30s subunit, (2) the mRNA coding for the polypeptide to be made, (3) met-trnai, (4) initiation factors, and (5) GTP. (12 Dec 1998) |