کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10533461 | 961875 | 2012 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Design, synthesis, and characterization of chromogenic substrates of coagulation factor XIIIa
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
A series of Glu(pNA)-containing peptides was designed to determine the activity of the transglutaminase factor XIIIa at 405 nm due to p-nitroaniline release. The most suitable substrate properties were found for peptides containing the Glu(pNA) residue in the second position from the N terminus. For the best substrate 12 (H-Tyr-Glu(pNA)-Val-Lys-Val-Ile-Gly-NH2), a kcat/Km value of 3531 sâ1 Mâ1 was found. Although the kcat/Km values of the Glu(pNA) peptides are more than 100-fold reduced compared with the previously reported cleavage of natural glutamine-containing substrates such as α2-antiplasmin and β-casein, these chromogenic substrates can be useful tools for convenient determination of FXIII-A2â activity e.g., for in vitro inhibitor screening. As an example, peptide 12 was used to characterize the inhibition of FXIII-A2â by the well-known irreversible inhibitor iodoacetic acid.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Analytical Biochemistry - Volume 428, Issue 1, 1 September 2012, Pages 73-80
Journal: Analytical Biochemistry - Volume 428, Issue 1, 1 September 2012, Pages 73-80
نویسندگان
Kornelia Hardes, Gero Lutz Becker, M. Zouhir Hammamy, Torsten Steinmetzer,