کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9004944 | 1119683 | 2005 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
N-acetyl-β-d-hexosaminidase from Trichomonas vaginalis: substrate specificity and activity of inhibitors
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موضوعات مرتبط
علوم پزشکی و سلامت
پزشکی و دندانپزشکی
تومور شناسی
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چکیده انگلیسی
Among chitinolytic activities previously described in Trichomonas vaginalis, N-acetyl-β-d-hexosaminidase (NAHase) was the enzyme system expressing the highest level of specific activity. We report here some biochemical characteristics of NAHase purified from T. vaginalis. We found at first that the use of 4-methylumbellifferyl-substrate was responsible for a substrate affinity for the enzyme, about 1000-fold higher than those when using p-nitrophenyl-substrates (PNP). Whereas the optimum pH was 7.0 using PNP-substrate, it was at 4.5 using 4-methylumbelliferyl-substrate. Four different substrates were compared for their action on T. vaginalis NAHase and we have found that N-acetyl-β-d-glucosaminide substrate was the most specific. DTT had no effect on enzyme activity suggesting that thiol group are not involved at the catalytic site. The use of previously described inhibitors showed a positive correlation between trichomonacidal activity and NAHase inhibition.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biomedicine & Pharmacotherapy - Volume 59, Issue 5, June 2005, Pages 245-248
Journal: Biomedicine & Pharmacotherapy - Volume 59, Issue 5, June 2005, Pages 245-248
نویسندگان
A. Sanon, C. Tournaire-Arellano, S. Younes El Hage, C. Bories, R. Caujolle, P.M. Loiseau,