TY  - JOUR
AU  - Milosević, Maja S
AU  - Petrović, Snjezana B
AU  - Veličković, Nataša
AU  - Grković, Ivana S
AU  - Ignjatović, Marija
AU  - Horvat, Anica I
PY  - 2012
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/1084
AB  - Extracellular nucleotides affect female reproductive functions, fertilization, and pregnancy. The aim of this study was to investigate biochemical characteristics of ATP and ADP hydrolysis and identify E-NTPDases in myometrial cell membranes from Wistar albino rats. The apparent K (m) values were 506.4 +/- A 62.1 and 638.8 +/- A 31.3 mu M, with a calculated V (max) (app) of 3,973.0 +/- A 279.5 and 2,853.9 +/- A 79.8 nmol/min/mg for ATP and ADP, respectively. The enzyme activity described here has common properties characteristic for NTPDases: divalent cation dependence; alkaline pH optimum for both substrates, insensitivity to some of classical ATPase inhibitors (ouabain, oligomycine, theophylline, levamisole) and significant inhibition by suramine and high concentration of sodium azides (5 mM). According to similar apparent K-m values for both substrates, the ATP/ADP hydrolysis ratio, and Chevillard competition plot, NTPDase1 is dominant ATP/ADP hydrolyzing enzyme in myometrial cell membranes. RT-PCR analysis revealed expression of three members of ectonucleoside triphosphate diphosphohydrolase family (NTPDase 1, 2, and 8) in rat uterus. These findings may further elucidate the role of NTPDases and ATP in reproductive physiology.
T2  - Molecular and Cellular Biochemistry
T1  - ATP and ADP hydrolysis in cell membranes from rat myometrium
IS  - 1-2
VL  - 371
SP  - 248
EP  - 208
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_1084
ER  - 

@article{
author = "Milosević, Maja S and Petrović, Snjezana B and Veličković, Nataša and Grković, Ivana S and Ignjatović, Marija and Horvat, Anica I",
year = "2012",
abstract = "Extracellular nucleotides affect female reproductive functions, fertilization, and pregnancy. The aim of this study was to investigate biochemical characteristics of ATP and ADP hydrolysis and identify E-NTPDases in myometrial cell membranes from Wistar albino rats. The apparent K (m) values were 506.4 +/- A 62.1 and 638.8 +/- A 31.3 mu M, with a calculated V (max) (app) of 3,973.0 +/- A 279.5 and 2,853.9 +/- A 79.8 nmol/min/mg for ATP and ADP, respectively. The enzyme activity described here has common properties characteristic for NTPDases: divalent cation dependence; alkaline pH optimum for both substrates, insensitivity to some of classical ATPase inhibitors (ouabain, oligomycine, theophylline, levamisole) and significant inhibition by suramine and high concentration of sodium azides (5 mM). According to similar apparent K-m values for both substrates, the ATP/ADP hydrolysis ratio, and Chevillard competition plot, NTPDase1 is dominant ATP/ADP hydrolyzing enzyme in myometrial cell membranes. RT-PCR analysis revealed expression of three members of ectonucleoside triphosphate diphosphohydrolase family (NTPDase 1, 2, and 8) in rat uterus. These findings may further elucidate the role of NTPDases and ATP in reproductive physiology.",
journal = "Molecular and Cellular Biochemistry",
title = "ATP and ADP hydrolysis in cell membranes from rat myometrium",
number = "1-2",
volume = "371",
pages = "248-208",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_1084"
}

Milosević, M. S., Petrović, S. B., Veličković, N., Grković, I. S., Ignjatović, M.,& Horvat, A. I.. (2012). ATP and ADP hydrolysis in cell membranes from rat myometrium. in Molecular and Cellular Biochemistry, 371(1-2), 248-208.
https://hdl.handle.net/21.15107/rcub_ibiss_1084

Milosević MS, Petrović SB, Veličković N, Grković IS, Ignjatović M, Horvat AI. ATP and ADP hydrolysis in cell membranes from rat myometrium. in Molecular and Cellular Biochemistry. 2012;371(1-2):248-208.
https://hdl.handle.net/21.15107/rcub_ibiss_1084 .

Milosević, Maja S, Petrović, Snjezana B, Veličković, Nataša, Grković, Ivana S, Ignjatović, Marija, Horvat, Anica I, "ATP and ADP hydrolysis in cell membranes from rat myometrium" in Molecular and Cellular Biochemistry, 371, no. 1-2 (2012):248-208,
https://hdl.handle.net/21.15107/rcub_ibiss_1084 .