| SPARC | cysteine-rich acidic secreted protein |
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| MAP | malignant atrophic papulosis; mandibular angle plane; maturation-activated protein; maximal aerobic ... |
| MBP | major basic protein; maltose-binding protein; management by policy; mannose-binding protein; mean bl... |
| RP | radial pulse; radiopharmaceutical; rapid processing [of film]; Raynaud phenomenon; reactive protein;... |
| CPI | California Personality Inventory; Cancer Potential Index; congenital palatopharyngeal incompetence; ... |
| cysteine conjugate transaminase | <enzyme> Generates thiopyruvates by deamination of cysteine conjugates leaving the r-s-c bond intact Registry number: EC 2.6.1.- Synonym: cysteine-conjugate alpha-ketoglutarate transaminase (26 Jun 1999) |
|---|---|
| cysteine desulfhydrase | <enzyme> A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyses the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. Chemical name: L-Cystathionine cysteine-lyase (deaminating) Registry number: EC 4.4.1.1 (12 Dec 1998) |
| cysteine desulfurase | <enzyme> Pyridoxal phosphate enzyme which catalyses the formation of l-alanine and elemental sulfur from cysteine; required for full activation of the metalloproteins of azotobacter vinelandii nitrogenase Registry number: EC 4.4.1.- Synonym: nifs gene product, azotobacter, nifs protein, azotobacter (26 Jun 1999) |
| cysteine proteinase | <enzyme> An enzyme that destroys proteins by hydrolysis, turning them back into individual amino acids. (09 Oct 1997) |
| cysteine proteinase inhibitors | Exogenous and endogenous compounds which inhibit cysteine proteinases. (12 Dec 1998) |
| cysteine proteinases | <enzyme> Peptide hydrolases which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by sulfhydryl reagents. Registry number: EC 3.4.22 (12 Dec 1998) |
| cysteine S-conjugate N-acetyltransferase | <enzyme> Catalyses n-acetylation of l-cysteine thioesters to form mercapturic acids; important in drug detoxication Registry number: EC 2.3.1.80 Synonym: cscn acetyltransferase (26 Jun 1999) |
| cysteine sulfinate desulfinase | <enzyme> Catalyses removal of elemental sulfur and selenium atoms from cysteine, cystine, selenocysteine and selenocystine to produce l-alanine. Registry number: EC 4.4.1.- (26 Jun 1999) |
| cysteine sulfinic acid | -O2S-CH2CH (NH3)+COO-;a natural oxidation product of cysteine; an intermediate in the formation of taurine (via cysteic acid). (05 Mar 2000) |
| cysteine synthase | <enzyme> An enzyme that catalyses the biosynthesis of cysteine in microorganisms and plants from o-acetyl-l-serine and hydrogen sulfide. Chemical name: O(3)-Acetyl-L-serine acetate-lyase (adding hydrogen sulfide) Registry number: EC 4.2.99.8 (12 Dec 1998) |
| Onchocerca volvulus L3 cysteine protease | <enzyme> Required for molting of o. Volvulus third stage larvae; genbank u71150 Registry number: EC 3.4.22.- Synonym: cysteine protease l3, o volvulus, lovcp (26 Jun 1999) |
| L-cysteine-cystine C-S lyase | <enzyme> C-des - cysteine desulfhydrase; a pyridoxal phosphate- containing enzyme from synechocystis involved information of fe-s cluster of ferredoxin; catalyses the breakdown of l-cysteine to yield sulfide, pyruvate and ammonia; increased activity with cystine, yielding cysteine persulfide as the primary product; mw about 43 kD Registry number: EC 4.4.1.- Synonym: c-des lyase (26 Jun 1999) |
| acetoacetyl-acyl carrier protein synthase | <enzyme> E coli enzyme, that catalyses condensation of malonyl-acyl carrier protein plus acetyl-acyl carrier protein; not inhibited by cerulenin Registry number: EC 2.3.1.- Synonym: acetoacetyl-acp synthase (26 Jun 1999) |
| acid soluble spore protein | <molecular biology> A DNA binding protein in the spores of some bacteria, thought to stabilise the DNA in an A configuration, so protecting it from cleavage by enzymes or UV light. (18 Nov 1997) |
| acute-phase protein | <haematology> These plasma proteins (in addition to fibrinogen) increase 25% or more in response to inflammation and injury are under direct control of interleukin-6 (IL-6) (hepatocyte-stimulating factor). Other proteins which increase are ceruloplasmin, C3 and C4 which increase 50% or more; alpha-1 acid glycoprotein, alpha-1 antitrypsin, haptoglobin and fibrinogen (the major determinant of viscosity 1 ) which increase two- to fourfold; C-reactive protein (CRP) and serum amyloid A which increase several hundred-fold. Despite long-held clinical opinion to the contrary, available data indicate that neither ESR nor measurement of specific acute-phase reactants are useful in excluding underlying infection or inflammation regardless of the pretest probability. These proteins are secreted into the blood in increased or decreased quantities by hepatocytes in response to trauma, inflammation, or disease. They can serve as inhibitors or mediators of the inflammatory processes. Certain acute-phase proteins have been used to diagnose and follow the course of diseases or as tumour markers. See also: amyloid, c-reactive protein, erythrocyte sedimentation rate, viscosity. (25 Jun 1999) |