Wyniki wyszukiwania - Biblioteka Nauki

Nowa wersja platformy, zawierająca wyłącznie zasoby pełnotekstowe, jest już dostępna.
Przejdź na https://bibliotekanauki.pl

Ograniczanie wyników

Znaleziono wyników: 3

Liczba wyników na stronie

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych: nucleoside triphosphate

Sortuj według:

Ogranicz wyniki do:

Unusual nucleoside triphosphate donors for nucleoside kinases: 3'-deoxyadenosine-2'-triphosphate and 2'-deoxyadenosine-3'-triphosphate

100%

Krawiec K. , Kierdaszuk B. , Kalinichenko E. N. , Mikhailopulo I. A. , Shugar D.

nr 1

Two non-conventional analogues of ATP, 3'-deoxyadenosine-2'-triphosphate (3'-d-2'-ATP) and 2'-deoxyadenosine-3'-triphosphate (2'-d-3'-ATP), the syntheses of which are described, were examined as potential phosphate donors for the nucleoside kinases: 2'-deoxycytidine kinase (dCK), cytosolic thymidine kinase (TK1) and mitochondrial thymidine kinase (TK2). The reactions were monitored by means of a mixture of [γ-32P]ATP and cold analogue, andór with the use of 3H-labelled acceptors and cold donor. With dCK, using equimolar mixtures of ATP with each analogue, and dC as acceptor, phosphate transfer from 3'-d-2'-ATP and 2'-d-3'-ATP amounted to 34% and 14%, respectively. With each analogue used alone (each at concentration of 100 μM), phosphate transfer from 3'-d-2'-ATP was 55% that from ATP, and from 2'-d-3'-ATP 16%. With human TK2, and equimolar mixtures of [γ-32P]ATP with each of the analogues, and 1 μM dT as acceptor, there was no detectable transfer from either analogue. But, when each analogue was used alone, phosphate transfer attained 11% and 5%, respectively, that for ATP alone. With the low affinity form of human TK1, and dT as acceptor, only low phosphate transfer occurred with either analogue used alone. Both compounds exhibited Michaelis-Menten kinetics (with significantly lower Vmax than ATP), while ATP exhibited cooperative kinetics with all three kinases.

Nucleoside 5'-tetraphosphate hydrolase from human placenta

84%

Pietrowska-Borek M. , Szalata M. , Guranowski A.

Cellular and Molecular Biology Letters

1999

tom 04

nr 3

Structure-function studies of the phosphoryl-transfer enzyme: phosphoenolpyruvate carboxykinase

67%

Delbaere L. T. J. , Sudom A. M. , Prasad L. , Leduc Y. , Goldie H.

Cellular and Molecular Biology Letters

2003

tom 08

nr 2A