Pyrimidine salvage enzymes in entamoeba histolytica

Joint Authors

Hasan, Husayn F.
al-Jalabi, Qusayy

Source

Mu'tah Journal for Research and Studies : Natural and Applied Sciences Series

Issue

Vol. 8, Issue 5 (31 Dec. 1993), pp.199-208, 10 p.

Publisher

Mutah University Deanship of Academic Research

Publication Date

1993-12-31

Country of Publication

Jordan

No. of Pages

10

Main Subjects

Biology

Abstract EN

Extracts of Entamoeba histolytica were surveyed for the enzymes which catalyse pryimidine salvage.

Cytidine deaminase (EC.

3.5.4.5), uridine kinase (EC.

2.7.1.48), cytidine kinase (EC, 2.71.43) and thymidine Kinase (EC.

2,7.1.75) were all detected at relatively high activities, whereas, cytosine deaminase (EC.

3.5.4.1) and anabolic phos-phorylase were not detected.

Catabolic phosphoiylase (EC.

2.4.2.3) was found to be active only on uridine.

Uracil phosphoribosyl transferase (EC.

2.4.2.9) also was detected but, only at low activity.

The results suggest that in E.

histolytica the main route of pyrimidine nucleotide synthesis is through the action of kinases.

American Psychological Association (APA)

Hasan, Husayn F.& al-Jalabi, Qusayy. 1993. Pyrimidine salvage enzymes in entamoeba histolytica. Mu'tah Journal for Research and Studies : Natural and Applied Sciences Series،Vol. 8, no. 5, pp.199-208.
https://search.emarefa.net/detail/BIM-397569

Modern Language Association (MLA)

Hasan, Husayn F.& al-Jalabi, Qusayy. Pyrimidine salvage enzymes in entamoeba histolytica. Mu'tah Journal for Research and Studies : Natural and Applied Sciences Series Vol. 8, no. 5 (Dec. 1993), pp.199-208.
https://search.emarefa.net/detail/BIM-397569

American Medical Association (AMA)

Hasan, Husayn F.& al-Jalabi, Qusayy. Pyrimidine salvage enzymes in entamoeba histolytica. Mu'tah Journal for Research and Studies : Natural and Applied Sciences Series. 1993. Vol. 8, no. 5, pp.199-208.
https://search.emarefa.net/detail/BIM-397569

Data Type

Journal Articles

Language

English

Notes

Includes bibliographical references : p. 207-208

Record ID

BIM-397569