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001-es BibID:	BIBFORM078151
035-os BibID:	(PMID)1527783
Első szerző:	Balajthy Zoltán (biokémikus, sejtbiológus)
Cím:	Synthesis and functional evaluation of a peptide derivative of 1-beta-D-arabinofuranosylcytosine / Zoltán Balajthy, János Aradi, Ildikó T. Kiss, Pál Elődi
Dátum:	1992
Megjegyzések:	We have synthesized a peptidyl prodrug derivative of 1-beta-D-arabinofuranosylcytosine (1) designed to be a selective substrate of plasmin. D-Val-Leu-Lys-ara-C (2) was obtained by coupling the protected peptide Cbz-D-Val-Leu-(N6-Cbz)Lys-OH and ara-C (1) by a water-soluble carbodiimide (EDCI), followed by the removal of the Cbz groups by using catalytic hydrogenolysis over Pd/C. The kinetic constant of hydrolysis of 2 in the presence of plasmin demonstrated effective release of 1. The amino group of 1, which is sensitive to the removal by cytidine deaminase, is protected in 2 by the formation of the amide bond resulting in a prolonged half-life of 2 in biological milieu. The antiproliferative efficiency of 2 against L1210 leukemic cells was significantly higher than that of 1. The activity of 2 was abolished in the presence of serine proteinase inhibitor, (4-amidinopheny)methanesulfonyl fluoride. These data indicate that 2 is a prodrug form of 1 in systems generating plasmin.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Medicinal Chemistry. - 35 : 18 (1992), p. 3344-3349. -
További szerzők:	Aradi János (1942-) (biokémikus, vegyész) Kiss Ildikó (biokémikus) Elődi Pál (1927-2002) (biokémikus)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM078153
035-os BibID:	(PMID)2470217
Első szerző:	Zlateva, T. P.
Cím:	Properties of chymotrypsin bound covalently to dextran / Zlateva, T. P., Krysteva, M., Balajthy, Z., Elödi, P.
Dátum:	1988
Megjegyzések:	The kinetic properties dextran-chymotrypsin conjugate were studied by means of low molecular weight substrates. It was found that KM, kcat and kcat/KM of dextran chymotrypsin for the hydrolysis of benzoyl-L-tyrosine-ethyl-ester did not differ substantially from those of the free enzyme. However, the data found for kcat of dextran-chymotrypsin and free chymotrypsin assayed for the hydrolysis of three tripeptidyl-p-nitroanilide D-Arg-Val-Trp-pNA, D-Arg-Val-Tyr-pNA, Z-Phe-Pro-Phe-pNA, were definitely different. The inhibition of the modified chymotrypsin with soybean trypsin inhibitor was found to be less pronounced than that with the free enzyme. The effect of potassium and magnesium salts on the inactivation of both enzymes was also studied. The effect of dextran matrix on the catalytic properties and the conformational stability of modified chymotrypsin is discussed.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény hazai lapban
Megjelenés:	Acta Biochimica et Biophysica Hungarica. - 23 : 3-4 (1988), p. 225-230. -
További szerzők:	Krysteva, M. Balajthy Zoltán (1957-) (biokémikus, sejtbiológus) Elődi Pál (1927-2002) (biokémikus)
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