PubMed · 369200
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H J Eggers. 1978. [Progress in virostatic therapy].. https://pubmed.ncbi.nlm.nih.gov/369200/
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We have investigated conditions optimal for the conversion of L-lysine to its N6-hydroxy derivative by partially purified cell-free extracts of Aerobacter aerogenes 62-1. The enzyme system was highly specific to L-lysine: the D-isomer and, the N2- or N6-derivatives of lysine, and alpha-amino acids were not hydroxylated. Most of the latter compounds had little effect onthe hydroxylation of L-lysine. However, -l-glutamic acid and L-glutamine enhanced the hydroxylation, with half-maximal activation achieved at 100 micrometers concentration of the effector. The Km values for pyruvate and L-(+)-lactate (compounds known to stimulate N-hydroxylysine formation) were found to be approx. 100 micrometers. The data show that N-hydroxylation of the amino acid precedes acylation in the biosynthesis of hydroxamic acid in A. aerogenes 62-1.
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Successful cultivation and titration of Borna disease virus in cell cultures enabled detailed studies of the virus properties. Borna virus is labile towards treatment with heat, pH 3.0 and lipid solvents. It is relatively stable at low temperatures and in frozen state. It is easily inactivated by ultraviolet light as e.g. vesicular stomatitis virus. After ultrafiltration studies, the size of the infectious virus unit is between 80 and 100 nm. Its buoyant density in cesium chloride is 1.165 g per ml. The one step multiplication curve shows that Borna virus has a replication cycle of about 2 days in BSC 1 cells. In growth experiments using antimetabilites it behaves like certain RNA containing viruses. As its multiplication is not inhibited by bromo- and iododeoxyuridine and actinomycin D, no DNA step seems to be involved in virus synthesis. Regarding these properties and the intracellular antigen distribution as shown by fluorescent antibodies, it is not possible to attribute Borna virus to any of the established virus groups.