Single-column purification of syncephapepsin - An aspartic proteinase from Syncephalastrum racemosum

CMUR > College of Medicine > School of Medicine > Journal articles > Item 310903500/30359

Please use this identifier to cite or link to this item: http://ir.cmu.edu.tw/ir/handle/310903500/30359

Title:	Single-column purification of syncephapepsin - An aspartic proteinase from Syncephalastrum racemosum
Authors:	Ho, HC;Shiau, PF;Wu, SL
Contributors:	醫學院醫學系生化學科;China Med Coll, Sch Med, Dept Biochem, Taichung 40421, Taiwan
Date:	1998
Issue Date:	2010-09-24 14:53:57 (UTC+8)
Publisher:	ACADEMIC PRESS INC
Abstract:	A novel series of 6,7,2',3',4'-substituted-1,2,3,4-tetrahydro-2-phenyl-4-quinolones were synthesized and evaluated for interactions with tubulin and for cytotoxic activity against a panel of human tumor cell lines, including ileocecal carcinoma (HCT-8), breast cancer (MCF-7), lung carcinoma (A-549), epidermoid carcinoma of the nasopharynx (KB), renal cancer (CAKI-1), and melanoma cancer (SKMEL-2). Most compounds (18, 20, 22-27) showed potent cytotoxic and antitubulin effects. The most active compounds (23, 26, 27) demonstrated strong cytotoxic effects with ED50 values in the nanomolar or subnanomolar range in almost all tumor cell lines. Three active racemates (20, 22, 25) were separated into the enantiomers, and generally, the optically pure (-)-isomers (20a, 22a, 25a) exhibited greater biological activity than the racemates or (+)-isomers. Cytotoxicity and antitubulin activity were closely correlated, with the most active compounds (23, 26, 27) having effects comparable to those of colchicine, podophyllotoxin, and combretastatin A-4.
Relation:	PROTEIN EXPRESSION AND PURIFICATION 12(3):399-403
Appears in Collections:	[School of Medicine] Journal articles

Files in This Item:

There are no files associated with this item.