<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Larcher,G.</style></author><author><style face="normal" font="default" size="100%">Bouchara,J.P.</style></author><author><style face="normal" font="default" size="100%">Annaix,V.</style></author><author><style face="normal" font="default" size="100%">Symoens,F.</style></author><author><style face="normal" font="default" size="100%">Chabasse,D.</style></author><author><style face="normal" font="default" size="100%">Tronchin,G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Purification and characterization of a fibrinogenolytic serine proteinase from Aspergillus fumigatus culture filtrate</style></title><secondary-title><style face="normal" font="default" size="100%">FEBS Lett.</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">0</style></keyword><keyword><style  face="normal" font="default" size="100%">Activity</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">analysi</style></keyword><keyword><style  face="normal" font="default" size="100%">analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">article</style></keyword><keyword><style  face="normal" font="default" size="100%">AS</style></keyword><keyword><style  face="normal" font="default" size="100%">Aspergillus</style></keyword><keyword><style  face="normal" font="default" size="100%">at</style></keyword><keyword><style  face="normal" font="default" size="100%">chromatography</style></keyword><keyword><style  face="normal" font="default" size="100%">Chromatography,Liquid</style></keyword><keyword><style  face="normal" font="default" size="100%">culture</style></keyword><keyword><style  face="normal" font="default" size="100%">Culture Media</style></keyword><keyword><style  face="normal" font="default" size="100%">de</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrophoresis,Polyacrylamide Gel</style></keyword><keyword><style  face="normal" font="default" size="100%">enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">ET</style></keyword><keyword><style  face="normal" font="default" size="100%">evidence</style></keyword><keyword><style  face="normal" font="default" size="100%">Fibrinogen</style></keyword><keyword><style  face="normal" font="default" size="100%">France</style></keyword><keyword><style  face="normal" font="default" size="100%">Group</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">im</style></keyword><keyword><style  face="normal" font="default" size="100%">IS</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoelectric Point</style></keyword><keyword><style  face="normal" font="default" size="100%">isolation &amp; purification</style></keyword><keyword><style  face="normal" font="default" size="100%">journal</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">MEDIA</style></keyword><keyword><style  face="normal" font="default" size="100%">metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Weight</style></keyword><keyword><style  face="normal" font="default" size="100%">observed</style></keyword><keyword><style  face="normal" font="default" size="100%">ON</style></keyword><keyword><style  face="normal" font="default" size="100%">ph</style></keyword><keyword><style  face="normal" font="default" size="100%">Print</style></keyword><keyword><style  face="normal" font="default" size="100%">purification</style></keyword><keyword><style  face="normal" font="default" size="100%">regional</style></keyword><keyword><style  face="normal" font="default" size="100%">Research</style></keyword><keyword><style  face="normal" font="default" size="100%">Research Support</style></keyword><keyword><style  face="normal" font="default" size="100%">result</style></keyword><keyword><style  face="normal" font="default" size="100%">results</style></keyword><keyword><style  face="normal" font="default" size="100%">SB - IM</style></keyword><keyword><style  face="normal" font="default" size="100%">Serine</style></keyword><keyword><style  face="normal" font="default" size="100%">Serine Endopeptidases</style></keyword><keyword><style  face="normal" font="default" size="100%">Synthetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Temperature</style></keyword><keyword><style  face="normal" font="default" size="100%">Weight</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1992</style></year><pub-dates><date><style  face="normal" font="default" size="100%">10/8/1992</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">69</style></number><volume><style face="normal" font="default" size="100%">308</style></volume><pages><style face="normal" font="default" size="100%">65 - 69</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">A fibrinogenolytic proteinase has been isolated from Aspergillus fumigatus culture filtrate by ammonium sulfate precipitation followed by successive chromatographies on Sephadex G-75 and immobilized phenylalanine. The purified proteinase exhibited a molecular weight of about 33 kDa. When analysed by SDS-polyacrylamide gels containing co-polymerized fibrinogen, the proteinase appeared as a broad band at the top of the gels, which could correspond to polymerization of the enzyme, as suggested by SDS-PAGE analysis of the unboiled eluate. The isoelectric point was 8.75 and the enzyme was not glycosylated. Proteinase activity was optimum at pH 9 and between 37 and 42 degrees C, although a decrease in activity was observed above 37 degrees C. PMSF and chymostatin markedly inhibited the proteinase activity, and good kinetic constants were obtained for the synthetic substrate, N-Suc-Ala-Ala-Pro-Phe-pNA. These results provide direct evidence that this enzyme belongs to the chymotrypsin-like serine proteinase group</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">36640</style></custom1><section><style face="normal" font="default" size="100%">65</style></section></record></records></xml>