@article {Su-Xia:2003:0929-8665:581,
title = "Cloning and Expression of a New Rat Procarboxypeptidase B Gene in Escherichia Coli and Purification of Recombination Carboxypeptidase B",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2003",
volume = "10",
number = "6",
publication date ="2003-12-01T00:00:00",
pages = "581-590",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2003/00000010/00000006/art00007",
doi = "doi:10.2174/0929866033478627",
keyword = "cloning and expression, specific activity, rt-pcr, rat, recombinant carboxypeptidase b, procarboxypeptidase b, application, purification",
author = "Su-Xia, Li and Yu-Jian, ZHANG and Li-Ping, TIAN and Qin-Sheng, YUAN and Yi, GONG",
abstract = "A new coding sequence of the procarboxypeptidase B gene was obtained from SD rat fresh pancreas by RT-PCR and highly expressed in Escherichia coli in inclusion bodies. The folded procarboxypeptidase B was subjected to trypsin enzymatic cleavage to produce active carboxypeptidase B, subsequently, carboxypeptidase B was effectively purified with anion exchange chromatography DEAE-FF and hydrophobic interaction chromatography Octyl FF, as a result, 40 mg carboxypeptidase B per litre cell culture with specific activity 7.42 u / mg was achieved. Further research showed that the obtained recombinant carboxypeptidase B could substitute carboxypeptidase B isolated from pancreas.",
}