<?xml version="1.0" encoding="UTF-8" ?>

    <journal>
    <language>en</language>
    <journal_id_issn>2008-2835</journal_id_issn>
    <journal_id_issn_online>2008-4625</journal_id_issn_online>
    <journal_id_pii></journal_id_pii>
    <journal_id_doi></journal_id_doi>
    <journal_id_isnet></journal_id_isnet>
    <journal_id_iranmedex>276</journal_id_iranmedex>
    <journal_id_magiran>5669</journal_id_magiran>
    <journal_id_sid>11181</journal_id_sid>
    <pubdate>
	    <type>gregorian</type>
	    <year>>2011</year>
	    <month>>July-September</month>
	    <day></day>
    </pubdate>
    <volume>3</volume>
    <number>3</number>
    <publish_type>online</publish_type>
    <publish_edition>1</publish_edition>
    <article_type>fulltext</article_type>
    <articleset>

<article>
	<language>en</language>
	<article_id_issn></article_id_issn>
	<article_id_issn_online></article_id_issn_online>
	<article_id_pubmed>23408781</article_id_pubmed>
	<article_id_pii></article_id_pii>
	<article_id_doi></article_id_doi>
	<article_id_iranmedex></article_id_iranmedex>
	<article_id_magiran></article_id_magiran>
	<article_id_sid></article_id_sid>
	<title_fa></title_fa>
	<title>Expression and Purification of Functionally Active Recombinant Human Alpha 1-Antitrypsin in Methylotrophic Yeast Pichia Pastoris</title>
	<subject_fa></subject_fa>
	<subject></subject>
	<content_type_fa></content_type_fa>
	<content_type></content_type>
	<abstract_fa></abstract_fa>
	<abstract>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.</abstract>
	<keyword_fa></keyword_fa>
	<keyword>Alpha 1-antitrypsin, Pichia Pastoris, Protease inhibitors, Recombinant proteins</keyword>
	<start_page>127</start_page>
	<end_page>134</end_page>
	<web_url>https://www.ajmb.org/En/Article.aspx?id=66</web_url>
    <pdf_url>https://www.ajmb.org/PDF/En/FullText/66.pdf</pdf_url>
	<author_list><author><first_name>Sareh</first_name><middle_name></middle_name><last_name>Arjmand</last_name><suffix></suffix><affiliation>School of Pharmacy, Zanjan University of Medical Science, Zanjan, Iran</affiliation><first_name_fa></first_name_fa><middle_name_fa></middle_name_fa><last_name_fa></last_name_fa><suffix_fa></suffix_fa><email></email><code>244</code><coreauthor></coreauthor><affiliation_fa></affiliation_fa></author><author><first_name>Elham</first_name><middle_name></middle_name><last_name>Bidram</last_name><suffix></suffix><affiliation>Department of Clinical Biochemistry, Tarbiat Modares University, Tehran, Iran</affiliation><first_name_fa></first_name_fa><middle_name_fa></middle_name_fa><last_name_fa></last_name_fa><suffix_fa></suffix_fa><email></email><code>245</code><coreauthor></coreauthor><affiliation_fa></affiliation_fa></author><author><first_name>Abbas</first_name><middle_name></middle_name><last_name>Sahebghadam Lotfi</last_name><suffix></suffix><affiliation>Department of Clinical Biochemistry, Tarbiat Modares University, Tehran, Iran</affiliation><first_name_fa></first_name_fa><middle_name_fa></middle_name_fa><last_name_fa></last_name_fa><suffix_fa></suffix_fa><email></email><code>246</code><coreauthor></coreauthor><affiliation_fa></affiliation_fa></author><author><first_name>Mehdi</first_name><middle_name></middle_name><last_name>Shamsara</last_name><suffix></suffix><affiliation>National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran</affiliation><first_name_fa></first_name_fa><middle_name_fa></middle_name_fa><last_name_fa></last_name_fa><suffix_fa></suffix_fa><email></email><code>247</code><coreauthor></coreauthor><affiliation_fa></affiliation_fa></author><author><first_name>Seyed Javad</first_name><middle_name></middle_name><last_name>Mowla</last_name><suffix></suffix><affiliation>Department of Molecular Genetics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran</affiliation><first_name_fa></first_name_fa><middle_name_fa></middle_name_fa><last_name_fa></last_name_fa><suffix_fa></suffix_fa><email></email><code>248</code><coreauthor></coreauthor><affiliation_fa></affiliation_fa></author></author_list>
</article>

</articleset>
</journal>

