| APSAC | acylated plasminogen-streptokinase activator complex; anisoylated plasminogen streptokinase activato... |
|---|---|
| ARC | accelerating rate calorimetry; acquired immunodeficiency syndrome-related complex; active renin conc... |
| MAC | MacConkey [broth]; major ambulatory category; malignancy-associated changes; maximum allowable conce... |
| QRS | in electrocardiography, the complex consisting of Q, R, and S waves, corresponding to depolarization... |
| SFC | soluble fibrin complex; soluble fibrin-fibrinogen complex; spinal fluid count |
| pancreatic enzyme | <biochemistry> One of the proteins made by the pancreas that aid digestion of fats, carbohydrates and proteins. (09 Oct 1997) |
|---|---|
| malate-condensing enzyme | <enzyme> An important enzyme in the glyoxylic acid cycle which reversibly catalyses the synthesis of l-malate from acetyl-CoA and glyoxylate. Chemical name: L-Malate glyoxylate-lyase (CoA-acetylating) Registry number: EC 4.1.3.2 (12 Dec 1998) |
| malic enzyme | <enzyme> An enzyme that catalyses the conversion of (s)-malate and NAD+ to oxaloacetate and NADH. Chemical name: (S)-Malate:NAD+ oxidoreductase Registry number: EC 1.1.1.37 (12 Dec 1998) |
| pantoate-activating enzyme | pantothenate synthetase |
| marker enzyme | <enzyme> An enzyme that is used to identify a specific cell type, cell organelle, or cell component. (05 Mar 2000) |
| reducing enzyme | <enzyme> An enzyme that catalyses a reduction; since all enzymes catalyze reactions in either direction, any reductase can, under the proper conditions, behave as an oxidase and vice versa, hence the term oxidoreductase. For individual reductase's, see the specific names. Synonym: reducing enzyme. (05 Mar 2000) |
| regulatory enzyme | <biochemistry> An enzyme that regulatescertain functions due to its ability to undergoa change in its catalytic activity through modification of its structure. (09 Oct 1997) |
| relaxing enzyme | <biochemistry> Any of several enzymes, such ashelicase, that unwind DNA prior to its replication. (09 Oct 1997) |
| R enzyme | <enzyme> An enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullalan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Compare: isoamylase. Synonym: limit dextrinase, pullulanase, R enzyme. (05 Mar 2000) |
| repair enzyme | <enzyme, molecular biology> An enzyme that can catalyze the repair of damaged DNA; e.g., DNA ligase. (05 Mar 2000) |
| repressible enzyme | <biochemistry> In bacteria, an enzyme whose creation is inhibited when its reaction product is plentiful. (09 Oct 1997) |
| respiratory enzyme | One of those enzyme's in tissues that is a part of an oxidation-reduction system accomplishing the conversion of substrates to CO2 and H2O and the transfer of the electrons removed to O2. (05 Mar 2000) |
| respiratory enzyme complexes | <biochemistry> The enzymes that make up the respiratory chain: NADH Q reductase, succinate Q reductase, cytochrome reductase, cytochrome C and cytochrome oxidase. (18 Nov 1997) |
| glycogen debranching enzyme system | 1,4-alpha-d-glucan-1,4-alpha-d-glucan 4-alpha-d-glucosyltransferase/dextrin 6 alpha-d-glucanohydrolase. An enzyme system having both 4-alpha-glucanotransferase (ec 2.4.1.25) and amylo-1,6-glucosidase (ec 3.2.1.33) activities. As a transferase it transfers a segment of a 1,4-alpha-d-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-d-glucan. As a glucosidase it catalyses the endohydrolysis of 1,6-alpha-d-glucoside linkages at points of branching in chains of 1,4-linked alpha-d-glucose residues. Amylo-1,6-glucosidase activity is deficient in glycogen storage disease type III. (12 Dec 1998) |
| restriction enzyme | <enzyme, molecular biology> Class of bacterial enzymes that cut DNA at specific sites. In bacteria their function is to destroy foreign DNA, such as that of bacteriophages (host DNA is specifically modified at these sites). Type I restriction endonucleases occur as a complex with the methylase and a polypeptide that binds to the recognition site on DNA. They are often not very specific and cut at a remote site. Type II restriction endonucleases are the classic experimental tools. They have very specific recognition and cutting sites. The recognition sites are short, 4-8 nucleotides and are usually palindromic sequences. Because both strands have the same sequence running in opposite directions the enzymes make double stranded breaks, which, if the site of cleavage is off centre, generates fragments with short single stranded tails, these can hybridise to the tails of other fragments and are called sticky ends. They are generally named according to the bacterium from which they were isolated (first letter of genus name and the first two letters of the specific name). The bacterial strain is identified next and multiple enzymes are given Roman numerals. For example the two enzymes isolated from the R strain of E. Coli are designated Eco RI and Eco RII. (10 Mar 1998) |