A B S T R A C T We examined the vaginal washings from patients with nonspecific vaginitis (NSV) to seek biochemical markers and possible explanations for the signs and symptoms of this syndrome. Seven amines were identified including methylamine, isobutylamine, putrescine, cadaverine, histamine, tyramine, and phenethylamine. These amines may contribute to the symptoms of NSV and may contribute to the elevated pH of the vaginal discharge. They may also be partly responsible for the "fishy" odor that is characteristic of vaginal discharges from these patients. Among the seven amines, putrescine and cadaverine were the most abundant and were present in all vaginal discharges from each of ten patients before treatment. These amines are produced in vitro during growth of mixed vaginal bacteria in chemically defined medium, presumably by decarboxylation of the corresponding amino acids. We hypothesize that anaerobic vaginal organisms, previously shown to be quantitatively increased in NSV, are responsible for the amine production, because metronidazole inhibited the production ofamines by vaginal bacteria in vitro, and Haemophilus vaginalis did not produce amines. H. vaginalis did release high concentrations of pyruvic acid and of amino acids during growth in peptone-starch-dextrose medium, whereas, other vaginal flora consumed both pyruvic acid and amino acids in the same medium during growth. These findings suggest that a symbiotic relationship may exist between H. vaginalis and other vaginal flora in patients with NSV.

The complete amino-acid sequence was determined for a rabbit-antibody light chain of allotype b4. The light chain was recovered from approximately 20 g of homogeneous antibody to group C streptococcal carbohydrate, which was obtained from an immunized rabbit. Several enzymic digestions were used to obtain the overlapping peptides necessary for the sequence determination.The L chain has 210 amino-acid residues, as determined by sequence analysis, and a molecular mass of 23,060 daltons. This antibody light chain contains seven half-cystine residues characteristic of the kB light-chain class. The amino-terminal sequence was determined to be Ala-AspIle-Val-Met, indicating that the chain belongs to the VKI subgroup.

A rapid and specific procedure was developed for the simultaneous detection of bacterial acylases and P-lactamases, using ampicillin and cephalexin as substrates. Bacterial suspensions from agar plates were incubated separately with each l-lactam substrate for 1 h at 37°C. The supernatant of the reaction mixture was dansylated, and the dansyl derivatives were separated by two-dimensional thin-layer chromatography on polyamide sheets. The end products resulting from acylase hydrolysis, including the intact ,-lactam nucleus, 6-aminopenicillanic acid or 7-aminodeacetoxycephalosporanic acid, and the acyl side chain acid, D-(-)-aaminophenylacetic acid, and the end product resulting from P-lactamase hydrolysis (D-phenylglycylpenicilloic acid or D-phenylglycyldeacetoxycephalosporoic acid) were separated from each unhydrolyzed substrate and amino acids by this procedure. The presence of the intact P-lactam nucleus in the reaction mixture is the indication of acylase activity. This method is sensitive and reproducible and has been successfully applied to screening for acylase activity in a variety of bacteria. It may be pharmaceutically useful for identifying organisms capable of removing the acyl side chain from naturally occurring ,l-lactam antibiotics such as penicillin G, penicillin V, and cephalosporin C for production of the l-lactam nuclei which serve as the starting materials for semisynthetic ,l-lactam antibiotics.