1995
DOI: 10.1016/1357-2725(94)00076-n
|View full text |Cite
|
Sign up to set email alerts
|

Diadenosine 5′,5‴-P1,P4-tetraphosphate hydrolase is present in human erythrocytes, leukocytes and platelets

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
7
0

Year Published

1999
1999
2012
2012

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 15 publications
(7 citation statements)
references
References 15 publications
0
7
0
Order By: Relevance
“…The low K m value of wild-type enzyme indicated that the Plasmodium enzyme has high affinity for Ap 4 A; this high substrate affinity was previously observed for Ap 4 A hydrolase isolated from both human erythrocytes (K m 0.7 µM) and leukocytes (K m 1.5 µM). 24) Several studies of Nudix hydrolases have referred to the importance of catalytic residues inside and adjacent to the catalytic motif. The principles of this catalytic mechanism appear to be well conserved among the Nudix hydrolases, including those of humans.…”
Section: Discussionmentioning
confidence: 99%
“…The low K m value of wild-type enzyme indicated that the Plasmodium enzyme has high affinity for Ap 4 A; this high substrate affinity was previously observed for Ap 4 A hydrolase isolated from both human erythrocytes (K m 0.7 µM) and leukocytes (K m 1.5 µM). 24) Several studies of Nudix hydrolases have referred to the importance of catalytic residues inside and adjacent to the catalytic motif. The principles of this catalytic mechanism appear to be well conserved among the Nudix hydrolases, including those of humans.…”
Section: Discussionmentioning
confidence: 99%
“…Protein extracts obtained by ammonium sulphate fractionation (40-80%) of platelet homogenates exhibit hydrolase activity on e-(Ap 3 A) and e-(Ap 4 A) due to Ap 3 Aase and asymmetrical Ap 4 Aase, respectively. The presence of asymmetrical Ap 4 Aase in human blood cells has previously been reported [19,21]. Hydrolase activity on e-(Ap 2 A), the substrate used to detect non-specific phosphodiesterase activity, was negligible.…”
Section: Resultsmentioning
confidence: 74%
“…Enzyme purification. Concentrates of human platelets (700 ml) were processed to eliminate other contaminating blood cells and to fractionate platelet protein between 40% and 80% of ammonium sulphate saturation according to [19]. The protein pellet after 80% ammonium sulphate precipitation was redissolved in 50 mM Hepes KOH, pH 7.0, 0.1 M KCl, 5% glycerol (26 ml), divided into three aliquots and each subjected to gel-filtration chromatography on a Sephacryl S-200 column (26 mm´900 mm) equilibrated in the same buffer and eluted at 2.0 ml/min.…”
Section: Methodsmentioning
confidence: 99%
“…Since it has been demonstrated that the Ap 4 A hydrolase has limited specificity for the base and for whether the 2 -oxy or deoxy sugar is present, it was anticipated that it might be able to hydrolyze AZTp 4 A. Further, Ap 4 A hydrolase is widely distributed in mammalian tissues, having been identified in Ehrlich ascites tumor cells (Moreno et al, 1982), human leukemia cells (Ogilvie and Antl, 1983), human placenta (Lazewska et al, 1993), human erythrocytes, leukocytes, and platelets (Hankin et al, 1995). Hence, the metabolism of AZTp 4 A by Ap 4 A hydrolase could influence the effectiveness of AZT therapy.…”
Section: Discussionmentioning
confidence: 99%