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Acid phosphatases from latices of euphorbiaceae
Affiliation:1. Institute of Chemical Sciences, Gomal University, Dera Ismail Khan 29050, Pakistan;2. Department of Biochemistry, Women Medical and Dental College, Khyber Medical University KPK, Pakistan;3. National Key Laboratory of Crops Genetics and Improvement, PR China;4. Department of Chemistry, College of Science, Taif University, P.O. Box 11099, Taif 21944, Saudi Arabia;5. Department of Chemical Sciences, University of Lakki Marwat KPK, Pakistan;6. National Institute of Health Islamabad, Pakistan;7. Department of Physical Sport Science, College of Education, Princess Nourah bint Abdulrahman University, P.O. Box 84428, Riyadh 11671, Saudi Arabia
Abstract:Five phosphatases were isolated from the latices of three members of the Euphorbiaceae. From Euphorbia lathyris were obtained phosphatases 11 and 12; from E. trigona phosphatase t and from Elaeophorbia drupifera the enzymes d1 and d2. Phosphatases 11, 12 and t were purified to homogeneity. Amino acid compositions are reported and other properties of the enzymes are described. The two enzymes described from E. lathyris both have two pH maxima d(11 at 5.0 and 6.8,12 at 5.8 and 7.5) while t, d1 and d2 respectively have maxima at pHs of 5.6,5.6 and 5.0. On the basis of their responses to several residue-specific inhibitors the five phosphatases apparently comprise three groups: 12 and d1, t and d2, and 11.
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