Specific inhibition of procollagen C-endopeptidase activity by synthetic peptide with conservative sequence found in chordin.
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منابع مشابه
Specific inhibition of procollagen C-endopeptidase activity by synthetic peptide with conservative sequence found in chordin.
Procollagen C-endopeptidase (BMP-1) and N-endopeptidase (ADAMTS-2) are key enzymes for correct and efficient conversion of fibrillar procollagens to their self assembling monomers. Thus, they have an essential role in building and controlling the quality of extracellular matrices (ECMs). Here, we tested inhibition of activity of the largest variant of BMP-1, a recombinant mammalian tolloid (mTl...
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Procollagen C-endopeptidase (BMP-1) is one of two key enzymes crucial for conversion of fibrillar procollagens to self-assembling collagen monomers. Recently, we have reported inhibition of the largest variant of BMP-1, a recombinant mammalian tolloid (mTld) in vitro, on procollagen type I using peptides with amino acid sequences in chordin conserved across different species. Here, we tested th...
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In contrast to the wealth of information available concerning the response of plasma atrial natriuretic peptide to changes in pressure and volume status and to inhibition of endopeptidase 24.11, very little is known of possible concomitant effects on brain natriuretic peptide. The effects of change in posture, pressor infusions of angiotensin II, or inhibition of endopeptidase 24.11 were docume...
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The effect of synthetic rat C-peptide on glucose-induced insulin release was studied in isolated islets of rat pancreas. Addition of rat C-peptide II to the medium inhibited glucose-induced insulin release from islets by 30 to 40 percent. Rat C-peptide I, human connecting peptide and bovine, porcine and canine C-peptides had no significant effects on insulin release from islets of rat pancreas.
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ژورنال
عنوان ژورنال: Acta Biochimica Polonica
سال: 2008
ISSN: 1734-154X,0001-527X
DOI: 10.18388/abp.2008_3076