rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
10
|
pubmed:dateCreated |
1977-3-31
|
pubmed:abstractText |
Membrane bound LD-transpeptidase of Streptococcus faecalis ATCC 9790 was used to catalyse transpeptidation reactions between non radioactive peptide donors of the general type: L-Ala-D-Glu (L)meso-A2pm(L)-D-Ala and D-(14C) alanine acceptor. The presence of one or two amide residues on the carboxyl groups of glutamic acid and meso-diaminopimelic acid increases the transfer reactions and subsequently the yield in radioactive peptides L-Ala-D-Glu (L)meso-A2pm(L)-D-(14C) Ala.
|
pubmed:language |
fre
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0300-9084
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
58
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1167-72
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
|
pubmed:year |
1976
|
pubmed:articleTitle |
[Enzymatic preparation of peptides of the general type: L-Ala-D-Glu-L-mesodiaminopimelyl (L)-D (140) Ala by transfer reactions between non radioactive corresponding peptides and D-alanine (140)].
|
pubmed:publicationType |
Journal Article,
English Abstract
|