کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1214178 | 1494154 | 2010 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Digestive amylase of a primitive animal, the scorpion: Purification and biochemical characterization Digestive amylase of a primitive animal, the scorpion: Purification and biochemical characterization](/preview/png/1214178.png)
Scorpion, one of the most ancient invertebrates was chosen, as a model of a primitive animal, to purify and characterize an amylase located in the hepatopancreas. The scorpion digestive amylase (SDA) was purified. Pure SDA was obtained after heat treatment followed by ammonium sulfate fractionation and three steps of chromatography. The pure amylase is not glycosylated and has a molecular mass of 59,101 Da determined by MALDI-TOF MS analysis. The maximal amylase activity was measured at pH 7.0 and 50 °C, in the presence of Ca2+ and using potato starch as substrate. The enzyme was able to hydrolyze also, glycogen and amylose. The 23 NH2-terminal amino acid SDA residues were sequenced. The sequence obtained is similar to those of mammalian and avian pancreatic amylases. Nevertheless, polyclonal antibodies directed against SDA failed to recognize classical digestive amylases like the porcine pancreatic one.
Journal: Journal of Chromatography B - Volume 878, Issues 11–12, 1 April 2010, Pages 853–860