| recon | the smallest unit of DNA capable of recombination [recombination + Gr. on quantum] |
|---|---|
| ss(c)DNA | single-stranded circular deoxyribonucleic acid |
| ssDNA | single-stranded DNA |
| Z-DNA | zig-zag (left-handed helical) deoxyribonucleic acid |
| AAR | active avoidance reaction; acute articular rheumatism; antigen-antiglobulin reaction |
| PCR-SSP | Polymerase chain reaction-sequence specific primers |
|---|---|
| QPCR | Quantitative Polymerase Chain Reaction |
| Q/C PCR | Quantitative competitive polymerase chain reaction |
| QRT-PCR | Quantitative reverse transcriptase-polymerase chain reaction |
| QRT-PCR | Quantitative reverse transcription polymerase chain reaction |
| chain isomer | <chemistry> One of two or more compounds having the same chemical composition but differing in the arrangement of the atoms (usually carbon atoms) forming the backbone of the structure of the compounds. (21 Mar 1998) |
|---|---|
| chain reflex | A series of reflexs, each serving as a stimulus for the next. (05 Mar 2000) |
| phenylalanyl chain | A polypeptide component of insulin containing 30 amino acyl residues, beginning with a phenylalanyl residue (NH2-terminus); insulin is formed by the linkage of a B chain to an A chain by two disulfide bonds; the amino-acid composition of the B chain is a function of species. Synonym: phenylalanyl chain. (05 Mar 2000) |
| closed chain compound | Any compound in which the constituent atoms, or any part of them, form a ring. Used mainly in organic chemistry where: 1) numerous compound's contain rings of carbon atoms (carbocyclic compound's) or carbon atoms plus one or more atoms of other types (heterocyclic compound's), usually nitrogen, oxygen, or sulfur; 2) where the atoms in the ring are all of the same element (homocyclic or isocyclic compound); 3) where the ring is saturated or contains nonconjugated double bonds (alicyclic compound), the compound is similar in properties to the corresponding acyclic compound (e.g., cyclohexane resembles hexane); 4) where the ring contains conjugated double bonds in a closed loop in which there are 4n + 2 (where n is an integer) delocalised π electrons (Huckel's rule) (aromatic compound; e.g., benzene, pyridine), it is more stable than the corresponding saturated ring and exhibits unusual chemical properties characteristic of itself and not of other types of rings or of acyclic compound's. These aromatic compounds have the ability to sustain an induced ring current. Synonym: closed chain compound, ring compound. (05 Mar 2000) |
| cold chain | A system of protection against high environmental temperatures for heat-labile vaccines, sera and other biological preparations. (05 Mar 2000) |
| P light chain | <protein> Myosin light chain that can be phosphorylated by myosin light chain kinase, as a result of phosphorylation, the myosin is activated. (18 Nov 1997) |
| corticosteroid side-chain-isomerase | <enzyme> Converts 11-deoxycorticosterone to 20-hydroxy-3-oxypregn-4-en-21-al; also acts as an epimerase at c-20 Registry number: EC 5.3.1.21 Synonym: corticosteroid side chain isomerase, ccsci (26 Jun 1999) |
| MyoD heavy chain kinase | <enzyme> Required for actin activation of the magnesium atpase activity of dictyostelium myosin id (myod); specific for myod Registry number: EC 2.7.1.- Synonym: 110-kD protein kinase, dictyostelium, dictyostelium 110-kD protein (26 Jun 1999) |
| myosin heavy chain | <protein> See myosin: do not confuse with heavy meromyosin which is a subfragment of the heavy chain of myosin II. (18 Nov 1997) |
| myosin light chain | <protein> The light chains of the muscle protein myosin. Each molecule of myosin is composed of two heavy chains and two pairs of light chains. The light chains have a molecular weight of about 20 kD and there is one dissimilar pair of light chains associated with each heavy chain. The proteins all have sequence homology to calmodulin, but not all with calcium binding activity. Several types are known: regulatory light chains (LC 2, DNTB light chains) probably regulate the ATPase activity of the heavy chain directly (through the binding of calcium) or indirectly (activating when they themselves are phosphorylated by myosin light chain kinase) and essential light chains (LC 1, LC 3, alkali light chains), which have a more subtle and apparently nonessential role. In molluscan muscle the EDTA light chains (similar to LC 2 from vertebrate muscle) confer calcium sensitivity on the myosin itself. The light chains are "calmodulin-like" proteins that bind calcium. Two of them can be removed easily, and two with difficulty. The light chains bind the heavy chains in the vicinity of the head groups of the myosin. (12 Dec 1998) |
| myosin light chain kinase | <enzyme> An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and calmodulin. The 20-kD light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction. Chemical name: ATP:myosin-light-chain O-phosphotransferase Registry number: EC 2.7.1.117 (12 Dec 1998) |
| haemolytic chain | The haemolysis that occurs when complement is activated by the previously formed union of erythrocytes and specific antibody. (05 Mar 2000) |
| H chain | <protein> Heavy chain of immunoglobulin, see IgG, IgM, etc. (18 Nov 1997) |
| heavy chain | <protein> In general, the larger polypeptide in a multimeric protein. Thus the immunoglobulin heavy chain is of 50 kD, the light chain of 22 kD, whereas in myosin the heavy chain is very much larger (220 kD) than the light chains (~20 kD). (18 Nov 1997) |
| heavy chain disease | A disorder of immunoglobulin synthesis in which large quantities of abnormal heavy chains are excreted in the urine. The amino acid sequences of the n- (amino-) terminal regions of these chains are normal, but they have a deletion extending from part of the variable domain through the first domain of the constant region, so that they cannot form cross-links to the light chains. The defect arises through faulty coupling of the variable (v) and constant (c) region genes. (12 Dec 1998) |