Publications by authors named "K Radika"
The development of potent and selective urokinase-type plasminogen activator (uPA) inhibitors based on the lead molecule 2-(2-hydroxy-3-ethoxyphenyl)-1H-benzimidazole-5-carboxamidine (3a) is described.
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- New inhibitors targeting serine proteases have been created to bind specifically to the catalytic site Ser195 via short hydrogen bonds.
- These inhibitors are based on a lead molecule, 2-(2-hydroxyphenyl)1H-benzoimidazole-5-carboxamidine (6b), which can bind in different ways, including without zinc, by forming multiple hydrogen bonds.
- Optimized versions of these compounds, such as 22a and 22f, show strong potency against human serine proteases, with binding affinities ranging from 8 to 600 nM, and their binding mechanisms resemble that of the original lead molecule.
Expression, purification, and characterization of deglycosylated human pro-prostate-specific antigen.
Protein Expr Purif
December 2000
Wild-type and deglycosylated forms of human prostate-specific antigen were expressed in Chinese hamster ovary (CHO) cells as zymogens. ProPSA was collected from conditioned medium and purified using a single cation-exchange chromatographic step for the deglycosylated form and cation-exchange followed by gel filtration chromatography for the wild-type form. Recombinant wild-type proPSA produced in CHO cells has an average MW of 34.
View Article and Find Full Text PDFBackground: Urokinase-type plasminogen activator (uPA) is a protease associated with tumor metastasis and invasion. Inhibitors of uPA may have potential as drugs for prostate, breast and other cancers. Therapeutically useful inhibitors must be selective for uPA and not appreciably inhibit the related, and structurally and functionally similar enzyme, tissue-type plasminogen activator (tPA), involved in the vital blood-clotting cascade.
View Article and Find Full Text PDFUDP-N-acetylglucosamine acyltransferase of Escherichia coli catalyzes the reaction, UDP-GlcNAc + R-3-hydroxymyristoyl-ACP--> UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc + ACP. Using Matrex Gel Green A and heparin-agarose, we have purified the enzyme to near homogeneity from a strain that overproduces it 474-fold. The subunit molecular mass determined by SDS-gel electrophoresis is approximately 30 kDa, consistent with results of previous radiolabeling experiments in mini-cells.
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