| amylo-1,4:1,6-glucantransferase | 1,4-alpha-d-glucan branching enzyme |
|---|---|
| amylo-1,6-glucosidase | <enzyme> Catalyses endohydrolysis of 1,6-alpha-d-glucoside linkages at points of branching in chains of 1,4-linked alpha-d-glucose residues Registry number: EC 3.2.1.33 (26 Jun 1999) |
| amylobacter | <biology> A microorganism (Bacillus amylobacter) which develops in vegetable tissue during putrefaction. Origin: L. Amylum starch + NL. Bacterium. See Bacterium. Source: Websters Dictionary (01 Mar 1998) |
| amylocaine hydrochloride | 1-(Dimethylaminomethyl)-1-methylpropyl benzoate hydrochloride; benzoylethyldimethylaminopropanol hydrochloride;an early local anaesthetic once widely used but eventually abandoned because of side effects. (05 Mar 2000) |
| amyloclast | An obsolete term for amylase. Origin: amylo-+ G. Klastos, broken in pieces (05 Mar 2000) |
| amylodextrin | End product of hydrolysis of amylopectin by beta-amylase; further hydrolysis requires amylo-1,6-glucosidase, which attacks the branch points. Identified by its colour reaction with iodine (amylodextrin turns blue). Compare: achroodextrin, erythrodextrin. (05 Mar 2000) |
| amylogenesis | Biosynthesis of starch. Origin: amylo-+ G. Genesis, production (05 Mar 2000) |
| amylogenic | Relating to amylogenesis. (05 Mar 2000) |
| amylogenic body | A plant plastid involved in the synthesis and storage of starch. Found in many cell types, but particularly storage tissues. Characteristically has starch grains in the plastid stroma. (18 Nov 1997) |
| amyloglucosidase | A hydrolase removing terminal alpha-1,4-linked d-glucose residues from nonreducing ends of chains, with release of beta-d-glucose. Synonym: acid maltase, amyloglucosidase, gamma-amylase, glucoamylase. (05 Mar 2000) |
| amyloid | Glycoprotein deposited extracellularly in tissues in amyloidosis. The glycoprotein may either derive from light chain of immunoglobulin (AIO (amyloid of immune origin): 5-18 kD glycoprotein, product of a single clone of plasma cells, the N terminal part of lambda or kappa light chain) or, in what used to be referred to as AUO, amyloid of unknown origin, from serum amyloid A (SAA), one of the acute phase proteins that increases many fold in inflammation. The polypeptides are organised as a _ pleated sheet making the material rather inert and insoluble. Minor protein components are also found. Should be distinguished from _ amyloid deposited in the brain and that is derived from amyloid precursor protein (see amyloidogenic glycoprotein. (18 Nov 1997) |
| amyloid A-degrading serine protease | <enzyme> Reduced in amyloidosis associated with rheumatoid arthritis Registry number: EC 3.4.21.- Synonym: amyloid a-degrading activity, aad-protease (26 Jun 1999) |
| amyloid angiopathy | Deposition of acellular hyaline material in small arteries and arterioles of the leptomeninges and cerebral cortex in the elderly with resulting predilection for recurrent lobar intraparenchymal haematomas. (05 Mar 2000) |
| amyloid beta-protein | A 4 kD protein, 39-43 amino acids long, expressed by a gene located on chromosome 21. It is the major protein subunit of the vascular and plaque amyloid filaments in individuals with alzheimer's disease and in aged individuals with trisomy 21 (down syndrome). The protein is found predominantly in the nervous system, but there have been reports of its presence in non-neural tissue. (12 Dec 1998) |
| amyloid beta-protein precursor | A precursor to the amyloid-beta protein (beta/a4). Alterations in the expression of the amyloid beta-protein precursor (abpp) gene, located on chromosome 21, plays a role in the development of the neuropathology common to both alzheimer disease and down syndrome. Abpp is associated with the extensive extracellular matrix secreted by neuronal cells. Upon cleavage, this precursor produces three proteins of varying amino acid lengths: 695, 751, and 770. The beta/a4 (695 amino acids) or beta-amyloid protein is the principal component of the extracellular amyloid in senile plaques found in alzheimer disease, down syndrome and, to a limited extent, in normal aging. (12 Dec 1998) |