Biomedical subjects
Publications and source records attributed to J C Knight.
The three most readily accessible D-homo isomers of 17-acetoxy-6-methylpregna-4,6-diene-3,20-dione (Ib) have been prepared and characterized in detail. The 17-keto isomers IIb and IIIb were obtained by base-catalyzed rearrangement of Ia followed by reacetylation, and the 17a-ketone IVb by Lewis-Acid treatment of Ia.
A series of mutants which are blocked at various stages of the sterol degradative pathway have been isolated from the potent sterol degrader Mycobacterium fortuitum ATCC-6842. Sitosterol bioconversions by these mutants result in the accumulation of a number of intermediate compounds, some of which are potentially useful as substrates in the manufacture of medically important steroids. These intermediates include androst-4-ene-3,17-dione, androsta-1,4-diene,3,17-dione, ring A-degraded tricyclic compounds and various 9alpha-hydroxy-steroids.
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The two epimers of dihydrospectinomycin have been separated and identified structurally. Four tetrahydrospectinomycins have also been prepared.
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A mutant (UC9778) of M. fortuitum has been isolated which degrades cholesterol and plant sterols to mixtures of Ring A-phenolic compounds. The title compound was isolated by repeated chromatography, and its structure determined by spectroscopic methods.
Smallpox eradication culminated the most successful antimicrobial campaign in medical history. To characterize further the linear double-stranded DNA genome of the aetiological agent of smallpox, we have determined the entire nucleotide sequence of the highly virulent variola major virus, strain Bangladesh-1975 (VAR-BSH; 186,102 base pairs, 33.7% G + C; Genbank accession number, L22579). Here we highlight features of the molecule and focus on a few of the 187 putative proteins that probably contribute to pathogenicity and virus host-range properties. One hundred and fifty proteins were markedly similar to those of vaccinia virus (smallpox vaccine), for which a complete sequence has been reported for strain Copenhagen (VAC-CPN; 191,636 base pairs, 33.3% G + C). The remaining 37 proteins reflected variola-specific sequences or open reading frame divergences for variant proteins, which are often truncated or elongated compared with their vaccinia counterparts.