کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1938588 | 1050743 | 2007 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
MALDI mass sequencing and characterization of filarialglutathione-S-transferase
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Glutathione-S-transferase has been detected in the somatic extract and excretory–secretory products of different life stages of Setaria cervi, a bovine filarial parasite. The enzyme was subjected to MALDI-TOF followed by mass spectrometry and the nearest match found was Pleuronectes platessa GST. Molecular mass of the purified enzyme was≈26 kDa as determined by SDS–PAGE and MALDI-TOF. Setaria cervi GST exhibited high activity towards 1-chloro-2,4-dinitrobenzene and ethacrynic acid. Kinetic analysis with respect to 1-chloro-2,4-dinitrobenzene and glutathione as substrate revealed a Km of 2.22 mM and 0.61 mM, respectively. The activity was inhibited significantly by Cibacron blue and α-tocopherol.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 356, Issue 2, 4 May 2007, Pages 381–385
Journal: Biochemical and Biophysical Research Communications - Volume 356, Issue 2, 4 May 2007, Pages 381–385
نویسندگان
Sarika Gupta, Anchal Singh, Marshleen Yadav, Kalyan Singh, Sushma Rathaur,