کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7558883 | 1491381 | 2014 | 24 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Ultrasensitive internally quenched substrates of human cathepsin L
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Ultrasensitive internally quenched substrates of human cathepsin L Ultrasensitive internally quenched substrates of human cathepsin L](/preview/png/7558883.png)
چکیده انگلیسی
Internally quenched cathepsin L (Cat L) substrate ABZ-Bip-Arg-Ala-Gln-Tyr(3-NO2)-NH2 with high specificity constant (kcat/KMÂ =Â 2.6Â ÃÂ 107Â Mâ1Â sâ1) was synthesized. The resultant compound displayed high selectivity over other members of the cathepsin family (B, S, X, V, C, K, H, F, D, and A). Activity of Cat L at picomolar (pM) concentrations was found using this substrate. Moreover, it was established that the presence of the selective Cat L inhibitor suppressed the proteolysis of the substrate to a non-detectable level. Incubation of the synthesized compound with a cell lysate of healthy and cancer cell lines indicated significant differences in Cat L activity. Based on the obtained results, it is proposed that this substrate could be used for selective monitoring of Cat L activity in biological systems.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Analytical Biochemistry - Volume 466, 1 December 2014, Pages 30-37
Journal: Analytical Biochemistry - Volume 466, 1 December 2014, Pages 30-37
نویسندگان
Monika ÅÄgowska, Magdalena Wysocka, Timo Burster, MichaÅ PikuÅa, Krzysztof Rolka, Adam Lesner,