| DP | data processing; deep pulse; definitive procedure; degradation product; degree of polymerization; de... |
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| EDP | electron dense particle; electronic data processing; end-diastolic pressure |
| FEP | fluorinated ethylene-propylene; free erythrocyte protoporphyrin; front-end processing; front-end pro... |
| LISP | List Processing Language |
| PEP | peptidase; phospho(enol)pyruvate; peer evaluation program; phosphoenolpyruvate; pigmentation, edema,... |
| signal peptidase complex | A peptide present on proteins that are destined either to be secreted or to be membrane components. It is usually at the N terminus and normally absent from the mature protein. Normally refers to the sequence (ca 20 amino acids) that interacts with signal recognition particle and directs the ribosome to the endoplasmic reticulum where co translational insertion takes place. Could also refer to sequences that direct post translational uptake by organelles. Signal peptides are highly hydrophobic but with some positively charged residues. The signal sequence is normally removed from the growing peptide chain by signal peptidase, a specific protease located on the cisternal face of the endoplasmic reticulum. See: signal recognition particle. (18 Nov 1997) |
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| N-acetylaspartylglutamate peptidase | <enzyme> Produces glutamate plus n-acetylaspartate; found throughout rat CNS Registry number: EC 3.4.13.- Synonym: naag peptidase (26 Jun 1999) |
| N-benzyloxycarbonylglycyl-glycyl-arginyl peptidase | <enzyme> Enzyme from bacteroides gingivalis is a cysteine proteinase; enzyme from human serum which acts on the same substrate is a serine proteinase Registry number: EC 3.4.22.- Synonym: n-cbz-gly-gly-arg peptidase, cgga peptidase (26 Jun 1999) |
| dipeptidyl peptidase | A hydrolase occurring in two forms: Dipeptidyl peptidase I, dipeptidyl transferase, cleaving dipeptides from the amino end of polypeptides, dipeptidyl peptidase II, with properties similar to those of I, has a different specificity. (05 Mar 2000) |
| tri-alanyl peptidase | <enzyme> Biliary tract enzyme Registry number: EC 3.4.- (26 Jun 1999) |
| type IV prepilin peptidase | <enzyme> Product of the pulc-o pullulanase secretion gene operon; involved in processing prepilin signal peptide; may also function as an n-methyltransferase Registry number: EC 3.4.99.- Synonym: pulo protein, pulo gene product, pulo peptidase (26 Jun 1999) |
| FALGPA peptidase | <enzyme> An endopeptidase from treponema denticola that cleaves furylacryloyl-leu-gly-pro-ala; also active on bradykinin Registry number: EC 3.4.24.- Synonym: falgpa-peptidase (26 Jun 1999) |
| lysine-C peptidase | <enzyme> Used in amino acid sequence determinations Registry number: EC 3.4.99.- Synonym: lysine specific peptidase (26 Jun 1999) |
| antigen processing | Modification of an antigen by accessory cells. This usually involves endocytosis of the antigen and either minimal cleavage or unfolding. The processed antigen is then presented in modified form by the accessory cell. (18 Nov 1997) |
| automatic data processing | Data processing largely performed by automatic means. (12 Dec 1998) |
| batch processing | <technique> Growth in a closed system with a specific amount of nutrient medium. In bioprocessing, defined amounts of nutrient material and living matter are placed in a bioreactor and removed when the process is completed. (14 Nov 1997) |
| calcium-independent processing protease | <enzyme> Converts hiv-1 gp160 precursor to gp120 and gp41 Registry number: EC 3.4.- Synonym: viral envelope glycoprotein maturase, vem enzyme (26 Jun 1999) |
| gp160 processing protease | <enzyme> Converts hiv gp160 to gp120 and gp41, cleaving between arg511 and ala512 Registry number: EC 3.4.99.- (26 Jun 1999) |
| RNA processing | <molecular biology> Modifications of primary RNA trancripts including splicing, cleavage, base modification, capping and the addition of poly A tails. See: RNA editing. (23 Aug 1998) |
| RNA processing, post-transcriptional | Post-transcriptional biological modification of messenger, transfer, or ribosomal rnas or their precursors. It includes cleavage, methylation, thiolation, isopentenylation, pseudouridine formation, conformational changes, and association with ribosomal protein. (12 Dec 1998) |