Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2003-7-2
pubmed:abstractText
Many angiotensin converting enzyme inhibitory peptides (ACEIP) have been identified in recent years. Among all the literatures available thus far, almost all the ACEIP were obtained by means of enzymatic hydrolysis. However, little information was available on antihypertensive peptides obtained by DNA recombination technology. In the present paper, our aims were 1) to establish a new method to produce antihypertensive peptides (AHP), and 2) to study the expression profiles of different host strains (Escherichia coli JM109 and DH5alpha). To achieve these objectives, a DNA fragment encoding the published ACEIP, identified as FFVAPFPEVFGK (known as CEI12) was synthesized, ligated with the expression vector, pQE16, and transformed into E. coli JM109 and DH5alpha. SDS-PAGE analysis and Western-blotting detection demonstrated that the peptide CEI12 (fused with dihydrofolate reductase [DHFR]) was specifically expressed only in E. coli JM109 with IPTG induction. The expression profiles of the AHP CEI12 at different IPTG concentrations and different inducing times demonstrated no significant differences by SDS-PAGE analysis. The expression level of CEI12 (fused with DHFR) was about 500 microg/L culture.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-0302
pubmed:author
pubmed:issnType
Print
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1927-31
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Expression of milk-derived antihypertensive peptide in Escherichia coli.
pubmed:affiliation
College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang, 150030, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't