| ECG | Electro-Cardio-Graphy(-Gram); ½ÉÀüµµ = EKG 1. Conducting System Structu... |
|---|---|
| Km | Michaelis-Menten constant |
| APSAC | 1) Acylating the Plasminogen Streptokinase Activated Complex 2) Anisoylat... |
| APSAC | acylated plasminogen-streptokinase activator complex; anisoylated plasminogen streptokinase activato... |
| ARC | accelerating rate calorimetry; acquired immunodeficiency syndrome-related complex; active renin conc... |
| Complex I | complex |
|---|---|
| complex C | complex |
| PIC | 1-plasmin inhibitor complex |
| OGDC | 2-oxo-glutarate dehydrogenase complex |
| PIC | 2-plasmin inhibitor plasmin complex |
| Michaelis complex | Binary complex of an enzyme. (05 Mar 2000) |
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| Victor-Michaelis-Menten equation | <chemistry> Equation derived from a simple kinetic model for a single-substrate non-cooperative enzyme-catalyzed reaction that successfully accounts for the hyperbolic adsorption isotherm) relationship between substrate concentration and reaction rate. V = Vmax x S/(S + Km), where V is the initial velocity of the reaction, Km is the Michaelis constant, Vmax is the maximum rate approached by very high substrate concentrations and S is the initial substrate concentration. Similar equations can be derived for conditions in which the product is present and for multisubstrate enzymes. Synonym: Victor-Michaelis-Menten equation. (12 Jul 2000) |
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| Michaelis constant | <chemistry> The true dissociation constant for the enzyme-substrate binary complex in a single-substrate rapid equilibrium enzyme-catalyzed reaction (usually symbolised by Ks), the concentration of the substrate at which half the true maximum velocity of an enzyme-catalyzed reaction is achieved (when velocities are measured under initial rate and steady state conditions). The ratio of rate constants (k2 + k3)/k1 in the single-substrate enzyme-catalyzed reaction: E + S &dblarr; ES &dblarr; E + products where E represents the free enzyme, S is the substrate, and ES is the central binary complex. The expression for the Michaelis constant will be more complex for multisubstrate reactions. An apparent Michaelis constant is a constant determined either under conditions that are not strictly steady state and initial rate or one that varies with the concentration of one or more cosubstrates. See: Michaelis-Menten equation. Synonym: Michaelis-Menten constant. (05 Mar 2000) |
| Michaelis-Gutmann body | <radiology> A rounded homogenous or concentrically laminated body, 1 to 10 u in diameter, containing calcium apatite and iron; found within macrophages in the bladder wall in malakoplakia. (12 Jul 2000) |
| Michaelis, Leonor | <person> German-U.S. Chemist, 1875-1949. See: Michaelis-Gutmann body, Michaelis constant, Michaelis-Menten constant, Michaelis-Menten equation, Michaelis-Menten hypothesis. (05 Mar 2000) |
| Michaelis-Menten constant | <chemistry> The true dissociation constant for the enzyme-substrate binary complex in a single-substrate rapid equilibrium enzyme-catalyzed reaction (usually symbolised by Ks), the concentration of the substrate at which half the true maximum velocity of an enzyme-catalyzed reaction is achieved (when velocities are measured under initial rate and steady state conditions). The ratio of rate constants (k2 + k3)/k1 in the single-substrate enzyme-catalyzed reaction: E + S &dblarr; ES &dblarr; E + products where E represents the free enzyme, S is the substrate, and ES is the central binary complex. The expression for the Michaelis constant will be more complex for multisubstrate reactions. An apparent Michaelis constant is a constant determined either under conditions that are not strictly steady state and initial rate or one that varies with the concentration of one or more cosubstrates. See: Michaelis-Menten equation. Synonym: Michaelis-Menten constant. (05 Mar 2000) |
| Michaelis-Menten equation | <chemistry> Equation derived from a simple kinetic model for a single-substrate non-cooperative enzyme-catalyzed reaction that successfully accounts for the hyperbolic adsorption isotherm) relationship between substrate concentration and reaction rate. V = Vmax x S/(S + Km), where V is the initial velocity of the reaction, Km is the Michaelis constant, Vmax is the maximum rate approached by very high substrate concentrations and S is the initial substrate concentration. Similar equations can be derived for conditions in which the product is present and for multisubstrate enzymes. Synonym: Victor-Michaelis-Menten equation. (12 Jul 2000) |
| Michaelis-Menten hypothesis | <chemistry> That a complex is formed between an enzyme and its substrate (the O'Sullivan-Tompson hypothesis), which complex then decomposes to yield free enzyme and the reaction products (Brown hypothesis), the latter rate determining the overall rate of substrate-product conversion. See: Michaelis-Menten constant, Michaelis-Menten equation. (05 Mar 2000) |
| aberrant complex | An anomalous electrocardiographic complex, more specifically an abnormal ventricular complex caused by abnormal intraventricular conduction of a supraventricular impulse. (05 Mar 2000) |
| activated complex | <chemistry> State of highest energy during a reaction. When reactants form the activated complex, bond breaking and bond formation is occurring. Synonym: transition state. (09 Jan 1998) |
| AIDS dementia complex | <immunology> A frequent cerebral condition in people with AIDS that results in the loss of cognitive capacity, affecting the ability to function in a social or occupational setting. Its cause has not been determined exactly, but may result from HIV infection of cells in the brain or an inflammatory reaction to such infection. (09 Oct 1997) |
| aids-related complex | A prodromal phase of infection with the human immunodeficiency virus (HIV). Laboratory criteria separating aids-related complex (arc) from aids include elevated or hyperactive B-cell humoral immune responses, compared to depressed or normal antibody reactivity in aids; follicular or mixed hyperplasia in arc lymph nodes, leading to lymphocyte degeneration and depletion more typical of aids; evolving succession of histopathological lesions such as localization of kaposi's sarcoma, signaling the transition to the full-blown aids. (12 Dec 1998) |
| alpha-keto acid dehydrogenase complex | See: alpha-keto acid dehydrogenase. Anaerobic dehydrogenase, an enzyme (usually a pyridinoenzyme) catalyzing the transfer of hydrogen from some metabolite to some acceptor molecule (e.g., NAD+, cytochrome) other than oxygen; e.g., lactate dehydrogenase's, isocitrate dehydrogenase's, and others in EC class 1, excluding those listed under aerobic dehydrogenase. (05 Mar 2000) |
| alpha-ketoglutarate dehydrogenase complex | alpha-ketoglutarate dehydrogenase |
| amygdaloid complex | Almond-shaped group of basal nuclei anterior to the inferior horn of the lateral ventricle of the brain, within the temporal lobe. The amygdala is part of the limbic system. (12 Dec 1998) |
| anomalous complex | A complex in the electrocardiogram differing significantly from the physiologic type in the same lead. (05 Mar 2000) |
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