کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1926707 | 1536467 | 2008 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Liberation of an N-terminal proline-rich peptide from the cryptic proteinase of fibronectin by auto-proteolysis
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Liberation of an N-terminal proline-rich peptide from the cryptic proteinase of fibronectin by auto-proteolysis Liberation of an N-terminal proline-rich peptide from the cryptic proteinase of fibronectin by auto-proteolysis](/preview/png/1926707.png)
چکیده انگلیسی
Fibronectin (Fn) is a modular glycoprotein present in both the extra-cellular matrix and blood plasma. It has a cryptic zinc-metalloproteinase activity (Fn-proteinase) in the gelatin-binding domain (GBD). The nature of the enzyme's substrates and the specificity of the peptide bonds cleaved are not yet precisely known. We used mass spectrometry to demonstrate the auto-proteolytic cleavage of Fn-proteinase. A 14-mer N-terminal peptide is the most important product released. This peptide has a very peculiar sequence, AAVYQPQPHPQPPP, demonstrating that Fn-proteinase cleaves after three consecutive proline residues.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 479, Issue 2, 15 November 2008, Pages 158-162
Journal: Archives of Biochemistry and Biophysics - Volume 479, Issue 2, 15 November 2008, Pages 158-162
نویسندگان
Maurice Pagano, Gilles Clodic, Gérard Bolbach, Magalie Michiel, Saliha Haddag, Michèle Reboud-Ravaux,