Cloning and expression of a new rat procarboxypeptidase B gene in Escherichia coli and purification of recombination carboxypeptidase B.

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.

journal_name

Protein Pept Lett

authors

Su-Xia L,Yu-Jian Z,Li-Ping T,Qin-Sheng Y,Yi G

doi

10.2174/0929866033478627

subject

Has Abstract

pub_date

2003-12-01 00:00:00

pages

581-90

issue

6

eissn

0929-8665

issn

1875-5305

journal_volume

10

pub_type

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