کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1976050 1060672 2007 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and characterization of two pepsins from the stomach of pectoral rattail (Coryphaenoides pectoralis)
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Purification and characterization of two pepsins from the stomach of pectoral rattail (Coryphaenoides pectoralis)
چکیده انگلیسی

Two pepsins (A and B) were purified from the stomach of pectoral rattail (Coryphaenoides pectoralis) by acidification, ammonium sulfate precipitation, gel filtration chromatography and anion exchange chromatography to obtain a single band on native-PAGE and SDS-PAGE. The purities of pepsin A and B were increased to 7.1- and 13.0-fold with approximately 5.7% and 2.2% yield, respectively. Pepsin A and B had the apparent molecular weights of 35 and 31 kDa, respectively, when analyzed using SDS-PAGE and Sephacryl S-200 gel filtration. Pepsin A and B showed maximal activity at pH 3.0 and 3.5, respectively, and had the same optimal temperature at 45 °C using hemoglobin as a substrate. Both pepsin A and B were stable in the pH range of 2.0–6.0 but were unstable at the temperatures greater than 40 °C. Activity of both pepsins was inhibited by pepstatin A and was activated by divalent cations, indicating pepsin characteristics. Activities of both pepsins continuously decreased as NaCl concentration increased (0–30%). The enzymes had high affinity and activity toward hemoglobin with Km and Kcat values of 98–152 μM and 32–50 S− 1, respectively. Purified pepsins generally showed the similar characteristics to other fish pepsins.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 147, Issue 4, August 2007, Pages 682–689
نویسندگان
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