| DME | degenerative myoclonus epilepsy; dimethyl diester; dimethyl ether; diphasic meningoencephalitis; dir... |
|---|---|
| EC | effective concentration; ejection click; electrochemical; electron capture; embryonal carcinoma; eme... |
| ED | early-decision [applicant]; early differentiation; ectodermal dysplasia; ectopic depolarization; eff... |
| EI | Edmonton injector; electrolyte imbalance; electron impact; electron ionization; emotionally impaired... |
| EIC | elastase inhibition capacity; enzyme inhibition complex |
| IUGR | Intrauterine growth restriction |
|---|---|
| PCR-RFLP | PCR restriction fragment length polymorphisms |
| RFLP | PCR)-Restriction fragment length polymorphism |
| PCR-RFLP | Polymerase Chain Reaction-Restriction Fragment Length Polymorphism |
| RFLP | Restriction Fragment Length Polymorphic |
| 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) |
| P enzyme | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |