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Characterization and purification of alkaline phosphatase from Elephas trogontherii (Steppe elephant) bone

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Title Characterization and purification of alkaline phosphatase from Elephas trogontherii (Steppe elephant) bone
 
Creator Demir, Yaşar
Yildirim, Safinur
Demir, Nazan
 
Subject Elephas trogontherii
Elephant
Bone
Alkaline phos-phatase
 
Description 182-185
Four isozymes of alkaline phosphatase (AP) were purified from Elephas trogontherii (Steppe elephant) from different locations in the bone (outer and inner peripheral, cytosolic, and integral) using Sephadex G-200 gel filtration and TEAE-cellulose anion-exchange chromatography. The specimen was obtained from Erzurum Museum and its age was approx. 0.3-0.5 million years old. No fungi or bacteria were present in the bone sample. The enzyme activity was determined by using p-nitrophenylphosphate as a substrate. SDS-PAGE of all the isozymes gave a single band at the same location. The molecular mass of the four isozymes as determined by using gel filtration was about 60 kDa. Optimum pHs for the four isozymes were between 8-8.5. The optimum temperatures of the isozymes were: outer peripheral, 37.5ºC, cytosolic, 37.5ºC, inner peripheral, 35ºC and integral, 40ºC. The values of Vmax and Km, as well different optimum temperatures indicated that isozymes were structurally different.
 
Date 2009-03-30T08:01:06Z
2009-03-30T08:01:06Z
2005-06
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/3522
 
Language en_US
 
Relation A 01 N 63/00, C 12 N
 
Publisher CSIR
 
Source IJBB Vol.42(3) [June 2005]