A tankönyvellátás változásai a rendszerváltozás után

<p>Percentage of each phylum present in fresh faecal samples collected from domesticated rabbits and rectal samples collected from wild rabbits together with the percentage of sequences which could not be classified within a particular phylum.</p

Total number of OTUs detected in each sample group.

<p>Total number of OTUs detected in each sample group.</p

Percentage of each phylum present in samples collected from the stomach, jejunum, caecum, appendicular caecum, proximal colon, distal colon and rectum of wild rabbits together with the percentage of sequences which could not be classified within a particular phylum.

<p>Data presented are the mean values of 5 samples per region.</p

Conserved sequence motifs of alipA and alipB and lipolytic enzymes from the GDSL family.

<p>Alignment of Pfam conserved domains. The accession numbers of the aligned sequences are for the following organisms: CAA47020, triacylglycerol lipase from <i>Photorhabdus luminescens</i>; AAC38796, outer membrane esterase from <i>Salmonella typhimurium</i>; AAB61674, lipase/esterase from <i>Pseudomonas aeruginosa</i> PAO1. Conserved motifs are highlighted. The possible catalytic triad (Serine (S), Aspartic acid (D), Histidine (H)) is shown at the top of the alignment whenever necessary.</p

Analysis of the proteins expressed in <i>Escherichia coli</i> TOP10 cells following purification on a 15% denaturing polyacrylamide gel.

<p>Lanes M, protein standards; 1, before induction with 1 mM IPTG; 2, after cells were induced with IPTG and grown at 37°C for 5 h; 3, recombinant protein purified under native conditions with the ProBond™ purification system. Arrows designate the positions of the proteins on the gels.</p

Maximum Parsimony tree of lipases.

<p>Protein sequences were aligned using the built-in ClustalW (default parameters), the tree was built using the Maximum Parsimony method with default parameters and 500 bootstrap replications.</p

Best matches obtained using BLASTN for the lipolytic genes identified in <i>Anaerovibrio lipolyticus</i> 5ST.

<p>Best matches obtained using BLASTN for the lipolytic genes identified in <i>Anaerovibrio lipolyticus</i> 5ST.</p

Best matches using BLASTP for the predicted amino acid sequence of lipolytic genes identified in <i>Anaerovibrio lipolyticus</i> 5ST.

<p>Best matches using BLASTP for the predicted amino acid sequence of lipolytic genes identified in <i>Anaerovibrio lipolyticus</i> 5ST.</p

Activity of lipases isolated from <i>Anaerovibrio lipolyticus</i> 5ST against different substrates.

<p>ND. Not detected.</p

Relative activity of lipases cloned from <i>Anaerovibrio lipolyticus</i> 5ST after incubation for one hour at 50, 60 or 70°C.

<p>The enzymes were incubated 1 h at 50, 60 and 70°C in 50 mM MES buffer (pH 6.5); the residual activities were measured with a standard assay against ρ-nitrophenyl caprylate (C8). The activity of the enzyme at 40°C was defined as 100%. Control activities at 40°C were 794, 564 and 793 U·mg⁻¹ protein for alipA, alipBss and alipC respectively).</p