Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 2
pubmed:dateCreated
2002-7-3
pubmed:abstractText
Human group IIA secretory phospholipase A(2) (hGIIA sPLA(2)) is reported to be involved in inflammation, since its expression level is enhanced under various inflammatory conditions. In this work, we report the total chemical synthesis of this enzyme (124 amino acids) by solid-phase method. The identity of the protein, in denatured or folded (7 disulphide bonds) forms, was confirmed by electrospray MS. Synthetic sPLA(2) possesses the same circular dichroism spectrum, enzymic activity in hydrolysing different phospholipid substrates, and inhibitory effect in thrombin formation from prothrombinase complex as the recombinant sPLA(2). Furthermore, LY311727, a reported specific hGIIA sPLA(2) inhibitor, is able to inhibit the synthetic and the recombinant enzymes with the same efficiency. This study demonstrates that chemically continuous solid phase synthesis is an alternative and less time-consuming approach to producing small, structurally folded and fully active proteins of up to 124 amino acids, such as hGIIA sPLA(2). Moreover, this technique provides more flexibility in analogue synthesis to elucidate their physiological functions and pathological effects.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-10206954, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-10468563, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-10514475, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-10563508, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-10567392, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-10652303, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-10931177, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-10966479, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-11031251, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-11080672, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-11080673, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-11080676, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-11080677, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-11106649, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-11456564, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-1631144, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-2327585, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-7664108, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-8106488, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-8200342, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-8421710, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-8647125, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-9223275, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-9352465, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-9388214, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-9421195, http://linkedlifedata.com/resource/pubmed/commentcorrection/11936952-9726985
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
365
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
505-11
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Total direct chemical synthesis and biological activities of human group IIA secretory phospholipase A2.
pubmed:affiliation
Laboratoire de Pharmacochimie Moléculaire, Université Paris 7-Denis Diderot, Case 7066, 2, Place Jussieu, 75251 Paris Cedex 05, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't