a simple, fast and commercial method for trypsin purification from bovine pancreas
نویسندگان
چکیده
trypsin is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins. trypsin has been used widely in various biotechnological processes. in this study trypsin was purified using two precipitation cut, 35% and 75% as saturation percent of ammonium sulfate solutions, tca precipitation (2.5% w/v), ph precipitation and finally affinity chromatography. this method could be used to obtain 2.8 g purified trypsin with specific activity 155 u/mg and 26% recovery from 1kg bovine pancreas. therefore, this method is a simple, fast and commercial method for scale-up of trypsin extraction from bovine pancreas.
منابع مشابه
extraction and acetylation of purified trypsin from bovin pancreas and study of some its physico-chemical properties
آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...
15 صفحه اولThe Basic Trypsin Inhibitor of Bovine Pancreas
A derivative of the basic pancreatic inhibitor which contained carboxamidomethyl groups on half-cystine residues 14 and 38 was incubated with trypsin and intact inhibitor at pH 5.5. The carboxamidomethyl derivative after separation from trypsin and intact inhibitor released only lysine when incubated with carboxypeptidase B. The derivative was oxidized with performic acid and a peptide correspo...
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عنوان ژورنال:
دامپزشکیجلد ۲۴، شماره ۱، صفحات ۳۳-۳۹
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