A photoaffinity inhibitor of aromatase.

Several 7 alpha-substituted 4-androstene-3,17-diones are potent inhibitors of the biosynthesis of estrogens, with the most effective being 7 alpha-(4'-amino)phenylthio-4-androstene-3,17-dione. An azide derivative of this 7 alpha-thioether compound has been prepared as a potential photoaffinity inhibitor. The enzyme kinetics of the azide analog were examined under both dark conditions and UV irradiation.

Substituted C19 steroid analogs as inhibitors of aromatase.

Various C19-steroidal derivatives have been synthesized and evaluated in biochemical assays for their ability to inhibit the biosynthesis of estrogens. Steroids with substitutions on the A or B ring were prepared by Michael addition of various thiol reagents to appropriate dienone intermediates. An in vitro assay using human placental microsomes was used to evaluate aromatase-inhibitory properties.

A deletion mutation in glucosephosphate isomerase (GPI Denton).

A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.