Formation of enterovirus-like particle aggregates by recombinant baculoviruses co-expressing P1 and 3CD in insect cellsBiotechnology Letters - Tập 25 - Trang 919-925 - 2003
Yu-Chen Hu, John Tsu-An Hsu, Jen-Huang Huang, Mei-Shang Ho, Yi-Chen Ho
The assembly of enterovirus requires the cleavage of P1 polyprotein by protease
3CD into individual structural proteins. Two recombinant baculoviruses were
constructed to encode P1 and 3CD of enterovirus 71 (EV71), respectively. The
expressed 3CD successfully cleaved P1 in vitro and in vivo. Also, the
co-infection in insect cells resulted in crystalline virus-like particle
structures morphological... hiện toàn bộ
Monoclonal antibody purification by affinity chromatography with ligands derived from the screening of peptide combinatory librariesBiotechnology Letters - Tập 25 - Trang 1545-1548 - 2003
S.A. Camperi, N.B. Iannucci, G.J. Albanesi, M. Oggero Eberhardt, M. Etcheverrigaray, A. Messeguer, F. Albericio, O. Cascone
The peptide, Ala-Pro-Ala-Arg (APAR), was selected from the screening of a
tetrapeptide combinatorial synthetic library as the ligand for affinity
purification of an anti-Granulocyte Macrophage-Colony Stimulating Factor
(GM-CSF) monoclonal antibody (Mab) developed in mouse ascitis. The affinity
chromatographic matrix obtained by attachment of APAR to agarose, having a
peptide density of 0.5 μmol ml... hiện toàn bộ
N-alkane biodegradation by a marine bacterium in the presence of an oleophilic nutrimentBiotechnology Letters - Tập 15 - Trang 637-640 - 1993
Laurent Rivet, Gilbert Mille, Anne Basseres, Alain Ladousse, Claude Gerin, Monique Acquaviva, Jean-Claude Bertrand
Hexadecane biodegradation by a marine bacterium has been investigated in the
presence of an oleophilic nutriment (INIPOL EAP 22). Hydrocarbon attack was only
observed after metabolism of the fatty acids present in the fertilizer. The
bacterium used up 95 % fatty acids in the first 24 hours. Hexadecane
biodegradation took place after 50 h incubation and reached 40 % after 360 h.
New differences between isoenzymes A and B from Candida rugosa lipaseBiotechnology Letters - - 1997
M.J. Herna´iz, J.M. Sa´nchez-Montero, J.V. Sinisterra
Water adsorption isotherms of pure lipases A and B from Candida rugosa are
different and can be used to distinguish between the isoenzymes. The maximum
esterification yield (50%, 20h) can be achieved at initial 0.9<1.0. Lipase B is
more stereoselective (49% yield, 98% enantiomeri excess) than lipase A (47%
yield, 72% enantiomerci excess) but both isoenzymes mainly esterify the (S)
2(4-isobutylphen... hiện toàn bộ