0000000000528343
AUTHOR
Michal Kempny
ChemInform Abstract: A Simple Preparation of Mono-tert-butyl Benzyloxycarbonyl-L-glutamates.
(1995). A SIMPLE PREPARATION OF MONO-tert-BUTYL BENZYLOXYCARBONYL-L-GLUTAMATES. Organic Preparations and Procedures International: Vol. 27, No. 3, pp. 378-380.
A SIMPLE PREPARATION OF MONO-tert-BUTYL BENZYLOXYCARBONYL-L-GLUTAMATES
(1995). A SIMPLE PREPARATION OF MONO-tert-BUTYL BENZYLOXYCARBONYL-L-GLUTAMATES. Organic Preparations and Procedures International: Vol. 27, No. 3, pp. 378-380.
Sulphonamide Antifolates Inhibiting Thymidylate Synthase. Synthesis, Enzyme Inhibition and Cytotoxicity
Synthesis and biological evaluation are described of seven new analogues (3-9) of two potent thymidylate synthase inhibitors, 10-propargyl-5,8-dideazafolate (1) and its 2-methyl-2-deamino congener ICI 198583 (2). While the new compunds 3 and 4 were analogues of 1 and 2, respectively, containing a p-aminobenzenesulfonyl residue in place of the p-aminobenzoic acid residue, the remaining 5 new compounds were analogues of 4 with the L-glutamic acid residue replaced by glycine (5), L-valine (6), L-alanine (7), L-phenylglycine (8) or L-norvaline (9). The new analogues were tested as inhibitors of thymidylate synthases isolated from tumour (Ehrlich carcinoma), parasite (Hymenolepis diminuta) and n…
New adsorbents for thymidylate synthase affinity chromatography
New affinity adsorbents, intended for chromatography of thymidylate synthase (EC 2.1.1.45) from different sources, consisting of p-[N-[(2-amino-4-hydroxy-6-quinazolinyl)-methyl]-N-2-propynylamino]benzoyl-γ-[α-(3-carboxypropylamino)]glutamyl-glutamyl immobilized either on macroporous copolymer of acrylonitrile and n-butyl acrylate or on macroporous polymer of acrylonitrile itself, both crosslinked with divinylbenzene and having aminoethyl groups, were obtained. Both adsorbents were found to be effective in dUMP-dependent binding of thymidylate synthase from regenerating rat liver.
Thymidylate synthases from Hymenolepis diminuta and regenerating rat liver: purification, properties, and inhibition by substrate and cofactor analogues.
Comparative studies of thymidylate synthases, isolated from the tapeworm, Hymenolepis diminuta, and regenerating liver of its host, rat, aimed at a possibility of specific inhibition of the helminthic enzyme, are presented. While similar in structure (dimers with monomer molecular masses of 33.7 kDa and 34.9 kDa, respectively) and parameters describing interactions with substrates and products, the tapeworm and rat enzymes differed in the dependences of reaction velocity on temperature (Arrhenius plots biphasic and linear, respectively). The tapeworm, compared with the host, enzyme was less sensitive to the competitive slow-binding inhibition by 5-fluoro-dUMP and its 2-thio congener, but eq…