European Journal of Zoological Research
Abstract
Author(s): Sahar Majdi, Abbas Sahebghadam Lotfi, Sajjad Papi, Mehdi Forouzandeh Moghadam, Zeinab Joneidi, Fatemeh Memari, Ladan Farzampanah, Masoud Negahdary
Alpha-1 Antitrypsin is one of the Serpins which in fact indicates a Glico protein with 12% carbohydrate. It contains
394 amino acids with molecular weight of 54 KDa which is synthesized in liver and secretes into plasma. Its original
performance is to inhibit Neutrophil Elastase and protect the tissues, especially against destructive effects of
Elastase during inflammation. Genetic (inherited) shortage of AAT results in pulmonary and hepatic illnesses.
Emphysema is one of the most important one. Hence, due to their widespread application in medicine and treating
the diseases in the perspective of various bacterial, plant, and yeast sources, great medical companies pay much
attention to the production of recombinants in proteins. Furthermore, due to Glycosylatedness of this protein and its
high molecular weight, every technique which may increase the expression output and recombinant proteins
secretion in yeast can be regarded as a helpful instrument in producing this medicine. The current study is going to
investigate the purity separation and determination of the properties and optimization of the alpha-1 Antitrypsin
expression in Saccharomyces cerevisiae. In order to separate and purify this protein, some properties such as
molecular mass, the amount and capacity of inhibiting are also measured. It is worth mentioning that the materials
and performing technique in the present study have been determined in the following order: strains, plasmids,
cultivation environments, transformation, protein property determination, and expression increase.
