Linked Life Data

12735467

Source:http://linkedlifedata.com/resource/pubmed/id/12735467

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2003-5-8
pubmed:abstractText
The recently discovered serine protease called tissue plasminogen activator (t-PA) enables efficient dissolution of blood clots. t-PA works by converting plasminogen into its active form, plasmin, dissolving the major component of blood clots, fibrin. The activation of plasminogen by t-PA is enhanced by the presence of fibrin, and this is probably due to the fact that both plasminogen and t-PA possess high affinity binding sites for fibrin. Besides fibrin, fibrin monomers and some fibrin(ogen) degradation products, certain synthetic polymers (for instance, poly-L-lysines) can provide the same stimulation of plasminogen activation. The recently developed high-performance monolithic-disk chromatography, HPMDC, could become the most convenient way to study biological pairs of interest. The inherent speed of HPMDC isolation facilitates the recovery of a biologically active product, since the exposure to putative denaturing influences, such as solvents or temperature, is reduced. The better mass transfer mechanism (convection rather than diffusion) allows to consider only the biospecific reaction as time limiting. The step-by-step modeling of hypothetical affinity pairs between t-PA and different types of oligo/polymer forms of linear and branched lysine derivatives obtained both by initiated polycondensation and solid-phase peptide synthesis using HPMDC seemed to be possible and a quite useful tool. The results of quantitative evaluation of such affinity interactions were compared with those established for natural affinity counterparts to t-PA (monoclonal antibodies, plasminogen, fibrinogen). The role of steric structure of lysine ligands was observed and analyzed. The results allowing to make the practical choice of affinity systems will be used for development of fast and efficient analytical and preparative methods for the downstream processes of recombinant production of this valuable enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
992
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-19
pubmed:dateRevised
2009-1-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
In vitro comparison of complementary interactions between synthetic linear/branched oligo/poly-L-lysines and tissue plasminogen activator by means of high-performance monolithic-disk affinity chromatography.
pubmed:affiliation
Institute of Macromolecular Compounds, Russian Academy of Sciences, St. Petersburg, Russia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't