Linked Life Data

17929575

Source:http://linkedlifedata.com/resource/pubmed/id/17929575

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2007-10-12
pubmed:abstractText
The gene coding for glutaryl-7-aminocephalosporic acid acylase (Gl7ACA acylase) of the bacterium Brevundimonas diminuta (BrdGl7ACA), a commercial enzyme widely used in modem biocatalytic technologies for manufacture of b-lactam antibiotics, was cloned. Efficient expression systems for producing a "native" recombinant BrdGl7ACA and its analogs modified by attaching affinity groups--the chitin-binding domain of chitinases A1 and hexahistidine sequence--were designed. It was demonstrated that both the recombinant hybrid proteins and the native Gl7ACA acylase produced in E. coli cells underwent a correct autoproteolytic processing with generation of functionally active enzymes and could be isolated with a high yield using one-step affinity chromatography.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0555-1099
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
462-70
pubmed:meshHeading
pubmed:articleTitle
[Cloning and expression of variants of the glutaryl-7-aminocephalosporic acid acylase of the bacterium Brevundimonas diminuta in Escherichia coli cells].
pubmed:publicationType
Journal Article, English Abstract