Pharmacokinetics of meloxicam following intravenous and oral administration in green iguanas (Iguana iguana).

Objective: To determine pharmacokinetics of meloxicam in healthy green iguanas following PO and IV administration and assess potential toxicity.

Animals: 21 healthy green iguanas (Iguana iguana).

Procedures: To assess pharmacokinetics, 13 iguanas were administered a single dose (0.

Processing of dengue type 4 and other flavivirus nonstructural proteins.

Dengue type 4 (DEN4) and other flaviviruses employ host and viral proteases for polyprotein processing. Most proteolytic cleavages in the DEN4 nonstructural protein (NS) region are mediated by the viral NS2B-NS3 protease. The N-terminal third of NS3, containing sequences homologous to serine protease active sites, is the protease domain.

Mutational analysis of the octapeptide sequence motif at the NS1-NS2A cleavage junction of dengue type 4 virus.

We have previously shown that proper processing of dengue type 4 virus NS1 from the NS1-NS2A region of the viral polyprotein requires a hydrophobic N-terminal signal and the downstream NS2A. Results from deletion analysis indicate that a minimum length of eight amino acids at the C terminus of NS1 is required for cleavage at the NS1-NS2A junction. Comparison of this eight-amino-acid sequence with the corresponding sequences of other flaviviruses suggests a consensus cleavage sequence of Met/Leu-Val-Xaa-Ser-Xaa-Val-Xaa-Ala.

Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins.

The cleavages at the junctions of the flavivirus nonstructural (NS) proteins NS2A/NS2B, NS2B/NS3, NS3/NS4A, and NS4B/NS5 share an amino acid sequence motif and are presumably catalyzed by a virus-encoded protease. We constructed recombinant vaccinia viruses expressing various portions of the NS region of the dengue virus type 4 polyprotein. By analyzing immune precipitates of 35S-labeled lysates of recombinant virus-infected cells, we could monitor the NS2A/NS2B, NS2B/NS3, and NS3/NS4A cleavages.

Plasmid-influenced changes in Mycobacterium avium catalase activity.

A virulent Mycobacterium avium strain, LR25, which carries three plasmids (18, 28, and 165 kilobases) and grows at 43 degrees C was compared with its plasmid-free, avirulent segregant, strain LR163, to identify the basis for the latter's inability to grow at 43 degrees C. The failure of mid-log-phase cultures of strain LR163 to grow at 43 degrees C was dependent on the presence of high levels of culture aeration. In addition, highly aerated cultures of strain LR163 failed to grow at 37 degrees C.