Expression and Purification of Functionally Active Recombinant Human Alpha 1-Antitrypsin in Methylotrophic Yeast Pichia pastoris

نویسندگان

  • Sareh Arjmand
  • Elham Bidram
  • Abbas Sahebghadam Lotfi
  • Mehdi Shamsara
  • Seyed Javad Mowla
چکیده

Human alpha 1-antitrypsin (AAT) cDNA was obtained from HepG2 cell lines. After PCR and construction of expression vector pPICZα-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 patterns 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.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Evaluation of pH/buffering conditions effect on the optimization of Recombinant Human Erythropoietin expression in the methylotrophic yeast, Pichia pastoris

Expression of recombinant proteins and drugs in Pichia pastoris has been in development since the late 1980s and the number of recombinant proteins produced in P. pastoris has increased significantly in the past several years. Unlike bacteria, this strain is capable of producing complex proteins with post translational modifications such as correct folding, glycosylation, proteolytic maturation...

متن کامل

P-65: Effective Parameters on the Bovine Follicle Stimulating Hormone Expression in The Pichia Pastoris System

Background: Bovine follicle-stimulating hormone (bFSH) is a heterodimer hormone that consists of a common -subunit which noncovalently associated with the hormone-specific -subunit. During the past 15 years, the methylotrophic yeast Pichia pastoris has become an important host organism for recombinant protein production because it is able to use methanol as a sole carbon and energy source. Th...

متن کامل

Expression of the VP2 gene of classical D78 infectious bursal disease virus in the methylotrophic yeast Pichia pastoris as a secretory protein

Infectious bursal disease virus (IBDV) is the causative agent of Gumboro disease, an infectious disease of global economic importance in poultry. The expression of heterologous proteins in P.pastoris is fast, simple and inexpensive. In this study, VP2 encoding gene of classical D78 IBDV was amplified using reverse transcription (RT) polymerase chain reaction (PCR) and cloned into pPICZαA vector...

متن کامل

Comparison of biochemical properties of recombinant phytase expression in the favorable methylotrophic platforms of Pichia pastoris and Hansenula polymorpha

Phytic acid is the dominant form of phosphorous in plant seeds. However, phytic acid cannot beutilized by animals and causes them serious phosphate deficiency. Utilization of phytase as ananimal feed additive can affect liberation of phosphor and its mineral availability. In this study,heterologous expression of the A. niger phyA gene was investigated in the methylotrophic yeastsP. pastoris and...

متن کامل

Elevating the expression level of biologically active recombinant human alpha 1-antitrypsin in Pichia pastoris

Background: Human alpha 1-antitrypsin (AAT) is a potent inhibitor of multiple serine proteases, and protects tissues against their harmful effects. Individuals with reduced or abnormal production of this inhibitor need intravenous administration of exogenous protein. In this study, we employed the methylotrophic (methanol utilizing) yeast Pichia pastoris (P. pastoris) as a preferential host for...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره 3  شماره 

صفحات  -

تاریخ انتشار 2011