False-positive urine beta-HCG in a woman with a tubo-ovarian abscess.

Modern urine beta-human chorionic gonadotropin (HCG) assays that use enzyme-linked immunosorbent assay (ELISA) technology are sensitive and specific for diagnosing pregnancy, both intrauterine and ectopic, and have become indispensable to the practice of Emergency Medicine. A urine HCG test is often relied on by the Emergency Physician as a critical component in the diagnostic regimen of a patient with a possible ectopic pregnancy. We report a case of a false-positive urine beta-HCG test in a patient with a ruptured tubo-ovarian abscess. Though false-positive pregnancy tests with tubo-ovarian abscesses have previously been reported with older methods of HCG detection, we believe that this is the first case where the pregnancy test was the modern ELISA type. The mechanism for the false-positive reaction in this case is unknown, but time may show that the ELISA test kit, like its predecessors, may occasionally give a false-positive reaction in this class of patients.

N omega-propargyl-L-arginine and N omega-hydroxy-N omega-propargyl-L-arginine are inhibitors, but not inactivators, of neuronal and macrophage nitric oxide synthases.

N omega-Propargyl-L-arginine (7) was synthesized as a potential mechanism-based inactivator of neuronal nitric oxide synthase (nNOS) and macrophage nitric oxide synthase (iNOS). Compound 7 is a potent reversible competitive inhibitor for both isoforms, having Ki values of 430 +/- 50 nM and 620 +/- 30 nM for nNOS and iNOS, respectively. These values are 12 and 32 times lower than the K(m) for L-arginine with nNOS and iNOS, respectively; however, 7 does not exhibit time-dependent inhibition with either. It also only undergoes oxidation very slowly. N omega-Hydroxy-N omega-propargyl-L-arginine also was synthesized to determine if the initial proposed enzyme-catalyzed hydroxylation of N omega-propargyl-L-arginine was problematic. This compound also is a potent reversible inhibitor of both nNOS and iNOS, but is not a time-dependent inactivator and is oxidized only very slowly. These results are in sharp contrast with the corresponding olefins, N omega-allyl-L-arginine and N omega-allyl-N omega-hydroxy-L-arginine recently reported to be potent time-dependent, irreversible inhibitors of nNOS (Zhang, H. Q.; Dixon, R. P.; Marletta, M. A.; Silverman, R. B., J. Am. Chem. Soc. 1997, 119, in press); N omega-allyl-L-arginine also was reported to be an inactivator of iNOS (Olken, N. M.; Marletta, M. A. J. Med. Chem. 1992, 35, 1137). This suggests that the active site of both isoforms of NOS can accommodate a variety of structures, but binding must have the appropriate juxtaposition for hydroxylation; otherwise, no oxidation occurs.