Pyrimidine salvage enzymes in entamoeba histolytica

المؤلفون المشاركون

Hasan, Husayn F.
al-Jalabi, Qusayy

المصدر

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

العدد

المجلد 8، العدد 5 (31 ديسمبر/كانون الأول 1993)، ص ص. 199-208، 10ص.

الناشر

جامعة مؤتة عمادة البحث العلمي

تاريخ النشر

1993-12-31

دولة النشر

الأردن

عدد الصفحات

10

التخصصات الرئيسية

الأحياء

الملخص 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.

نمط استشهاد جمعية علماء النفس الأمريكية (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

نمط استشهاد الجمعية الأمريكية للغات الحديثة (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

نمط استشهاد الجمعية الطبية الأمريكية (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

نوع البيانات

مقالات

لغة النص

الإنجليزية

الملاحظات

Includes bibliographical references : p. 207-208

رقم السجل

BIM-397569