Lüthje J - Search Results

1

Extracellular adenine compounds, red blood cells and haemostasis: facts and hypotheses.

Lüthje J. Lüthje J. Blut. 1989 Oct;59(4):367-74. doi: 10.1007/BF00321207. Blut. 1989. PMID: 2676021 Review.

2

Origin, metabolism and function of extracellular adenine nucleotides in the blood.

Lüthje J. Lüthje J. Klin Wochenschr. 1989 Mar 15;67(6):317-27. doi: 10.1007/BF01741386. Klin Wochenschr. 1989. PMID: 2651791 Review.

3

Demonstration of a novel ecto-enzyme on human erythrocytes, capable of degrading ADP and of inhibiting ADP-induced platelet aggregation.

Lüthje J, Schomburg A, Ogilvie A. Lüthje J, et al. Eur J Biochem. 1988 Aug 1;175(2):285-9. doi: 10.1111/j.1432-1033.1988.tb14195.x. Eur J Biochem. 1988. PMID: 2841133 Free article.

4

Catabolism of Ap4A and Ap3A in whole blood. The dinucleotides are long-lived signal molecules in the blood ending up as intracellular ATP in the erythrocytes.

Lüthje J, Ogilvie A. Lüthje J, et al. Eur J Biochem. 1988 Apr 5;173(1):241-5. doi: 10.1111/j.1432-1033.1988.tb13990.x. Eur J Biochem. 1988. PMID: 3356191 Free article.

5

Effects of diadenosine triphosphate (Ap3A) and diadenosine tetraphosphate (Ap4A) on platelet aggregation in unfractionated human blood.

Lüthje J, Baringer J, Ogilvie A. Lüthje J, et al. Blut. 1985 Dec;51(6):405-13. doi: 10.1007/BF00320727. Blut. 1985. PMID: 3852686

6

Identification and partial characterization of an adenosine(5')tetraphospho(5')adenosine hydrolase on intact bovine aortic endothelial cells.

Ogilvie A, Lüthje J, Pohl U, Busse R. Ogilvie A, et al. Among authors: luthje j. Biochem J. 1989 Apr 1;259(1):97-103. doi: 10.1042/bj2590097. Biochem J. 1989. PMID: 2541689 Free PMC article.

7

Unproportionally high concentrations of diadenosine triphosphate (Ap3A) and diadenosine tetraphosphate (Ap4A) in heavy platelets. Consequences for in vitro studies with human platelets.

Lüthje J, Miller D, Ogilvie A. Lüthje J, et al. Blut. 1987 Apr;54(4):193-200. doi: 10.1007/BF00594193. Blut. 1987. PMID: 3030468

8

Catabolism of Ap4A and Ap3A in human serum. Identification of isoenzymes and their partial characterization.

Lüthje J, Ogilvie A. Lüthje J, et al. Eur J Biochem. 1987 Dec 1;169(2):385-8. doi: 10.1111/j.1432-1033.1987.tb13624.x. Eur J Biochem. 1987. PMID: 2826143 Free article.

A hydrolase splitting adenosine (5')triphospho(5')adenosine (Ap3A) and adenosine(5')tetraphospho(5')adenosine (Ap4A) has recently been highly purified from human plasma [Luthje, J. and Ogilvie, A. (1985) Eur. J. Biochem. 149, 119-127]. ...

A hydrolase splitting adenosine (5')triphospho(5')adenosine (Ap3A) and adenosine(5')tetraphospho(5')adenosine (Ap4A) has recently been highl …

9

Catalytic activity concentrations of diadenosine tetraphosphate hydrolase in normal and pathological sera.

Lüthje J, Holler A, Ogilvie A, Siegfried W, Waldherr A, Domschke W. Lüthje J, et al. J Clin Chem Clin Biochem. 1987 Aug;25(8):493-8. doi: 10.1515/cclm.1987.25.8.493. J Clin Chem Clin Biochem. 1987. PMID: 2826640

10

Levels of 5'-nucleotide phosphodiesterase isoenzymes in normal and pathological sera.

Lüthje J, Pickert S, Ogilvie A, Hornemann E, Siegfried W, Waldherr A, Domschke W. Lüthje J, et al. Clin Chim Acta. 1988 Oct 14;177(2):131-9. doi: 10.1016/0009-8981(88)90134-9. Clin Chim Acta. 1988. PMID: 2853013

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