| PAL | pathology laboratory; peptidyl-alpha-hydroxyglycine alpha-amidating lysine phase alteration plane; p... |
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| LT | Cysteinyl-leukotrienes |
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| p-LTs | Peptide-leukotrienes |
| PPI | Peptidyl prolyl cis-trans-isomerase |
| PPIase | Peptidyl-prolyl cisltrans isomerase |
| PPIases | Peptidyl-prolyl isomerases |
| peptidyl leukotrienes | Leukotrienes having amino acids present (even single amino acids) although not true peptides; e.g., LTC4 is an S-substituted glutathione, LTD4 is an S-substituted cysteinylglycine, LTE4 is an S-substituted cysteine, and LTF4 (also known as gamma-glutamyl-LTE4) is an S-substituted gamma-glutamylcysteine. (05 Mar 2000) |
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| leukotrienes | A family of biologically active compounds derived from arachidonic acid by oxidative metabolism through the 5-lipoxygenase pathway. They participate in host defense reactions and pathophysiological conditions such as immediate hypersensitivity and inflammation. They have potent actions on many essential organs and systems, including the cardiovascular, pulmonary, and central nervous system as well as the gastrointestinal tract and the immune system. (12 Dec 1998) |
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| peptidyl-Asp metalloendopeptidase | <enzyme> Extracellular metalloproteinase secreted by a pseudomonas fragi mutant; partial amino acid sequence given in first source Registry number: EC 3.4.24.33 Synonym: endopeptidase asp-n (26 Jun 1999) |
| peptidyl-dipeptidase A | <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) |
| peptidyl-Lys metalloendopeptidase | <enzyme> From lysobacter enzymogenes; cleaves at the carboxyl side of lysine residues; active at pH 9;endoproteinase lys-c (EC 3.4.99.30) was combined with EC 3.4.24.20 in 1992 enzyme nomenclature Registry number: EC 3.4.24.20 Synonym: endoprotease lys-c, endopeptidase lys-c, endoproteinase lys-c, lysc protease (26 Jun 1999) |
| peptidyl prolyl cis trans isomerase | See: PPIase and immunophilin. (18 Nov 1997) |
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