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Expression and Purification of Functionally Active Recombinant Human Alpha 1-Antitrypsin in Methylotrophic Yeast Pichia pastoris
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نویسنده
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Arjmand Sareh ,Bidram Elham ,Sahebghadam Lotfi Abbas ,Shamsara Mehdi ,Mowla Javad
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منبع
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avicenna journal of medical biotechnology - 2011 - دوره : 3 - شماره : 3 - صفحه:127 -134
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چکیده
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Human alpha 1-antitrypsin (aat) cdna was obtained from hepg2 cell lines. after pcr and construction of expression vector ppiczá-aat, human aat was expressed in the yeast pichia pastoris (p.pastoris) in a secretary manner and under the control of inducible alcohol oxidase 1 (aox1) promoter. the amount of aat protein in medium was measured as 60 mg/l 72 hr after induction with methanol. results indicated the presence of protease inhibitory function of the protein against elastase. purification was done using his-tag affinity chromatography. due to the different patterns of glycosylation in yeast and human, the recombinant aat showed different sds-page pat- terns compared to that of serum-derived aat while pi shifted from 4.9 in native aat compared to 5.2 in recombinant aat constructed in this study.
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کلیدواژه
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Alpha 1-antitrypsin ,Pichia pastoris ,Protease inhibitors ,Recombinant proteins
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آدرس
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tarbiat modares university, Faculty of Biological Sciences, Department of Molecular Genetics, ایران. National Institute of Genetic Engineering and Biotechnology (NIGEB), ایران. zanjan university of medical sciences, School of Pharmacy, ایران, tarbiat modares university, Department of Clinical Biochemistry, ایران, tarbiat modares university, Department of Clinical Biochemistry, ایران. National Institute of Genetic Engineering and Biotechnology, ایران, National Institute for Genetic Engineering and Biotechnology (NIGEB), ایران, tarbiat modares university, Faculty of Biological Sciences, Department of Molecular Genetics, ایران
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پست الکترونیکی
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lotfi-ab@nigeb.ac.ir
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Authors
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