کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1987865 1540301 2009 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A Kazal-type serine proteinase inhibitor from chicken liver (clTI-1): Purification, primary structure, and inhibitory properties
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
A Kazal-type serine proteinase inhibitor from chicken liver (clTI-1): Purification, primary structure, and inhibitory properties
چکیده انگلیسی

Low-molecular-mass trypsin inhibitor (clTI-1; chicken liver Trypsin Inhibitor-1) was purified from chicken liver by extraction with perchloric acid, ammonium sulfate precipitation, a combination of ethanol-acetone fractionation followed by gel filtration, ion-exchange chromatography and RP-HPLC on a C18 column. The inhibitor occurs in two isoforms with molecular masses of 5938.56 and 6026.29 Da (determined by MALDI TOFF mass spectrometry). The complete amino acid sequences of both isoforms were determined (UniProtKB/Swiss-Prot P85000; ISK1L_CHICK). The inhibitor shows a high homology to Kazal-type family inhibitors, especially to trypsin/acrosin inhibitors and pancreatic secretory trypsin inhibitors. clTI-1 inhibits both bovine and porcine trypsin (Ka = 1.1 × 109 M−1 and 2.5 × 109 M−1, respectively). Significant differences were shown in the inhibition of the anionic and cationic forms of chicken trypsin (Ka = 4.5 × 108 M−1 and 1.2 × 1010 M−1). Weak interaction with human plasmin (Ka = 1.2 × 107 M−1) was also revealed.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 45, Issue 2, 1 August 2009, Pages 194–199
نویسندگان
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