Beta-lactamase producing Neisseria gonorrhea strains in Karachi.

Urethral or cervical swab of 255 patients attending Skin and Social Hygiene Centre and found positive for gram negative intracellular diplococci on direct microscopy were inoculated on Modified New York City (MNYC) medium and chocolate (heated blood) agar for isolation of neisseria gonorrhea. Growth of N. gonorrhea was obtained in 134 (52.5%) cases. These strains were tested for penicillin susceptibility by disc diffusion method and for the production of beta-lactamase by rapid penicillinase paper strip test and rapid chromogenic cephalosporin method. Penicillin resistance was found in 31 (23%) strains, of which twelve (9%) were beta-lactamase producers (PPNG), the remaining 19 (14%) strains were penicillin resistant beta-lactamase negative (Pen RB Neg). We conclude that PPNG as well as other penicillin resistant strains (Pen RB Neg) of neisseria gonorrhea are prevalent in our country and appropriate changes in the conventional therapeutic regime are desirable.

Identification of an ARF type low molecular mass GTP-binding protein in pea (Pisum sativum).

The ARF class of low molecular mass GTP-binding proteins, originally detected as cholera toxin-activated ADP-ribosylation factors (ARF) in mammalian cells, is now known to participate in intracellular membrane vesicle trafficking. We identified a GTP-binding protein in pea plumules which resembles ARF in several respects. Like mammalian ARF, the pea protein had an apparent molecular mass of 21 kDa and was distributed mainly (approximately 97%) in the cytosol, with 1% and 1.5% occurring in the Golgi and microsomal fractions, respectively. In comparison, small GTP-binding proteins in the 26-30 kDa range were enriched in membranous fractions. The 21 kDa protein crossreacted strongly with an ARF class I antibody prepared against a mammalian ARF, but did not crossreact with ARF 5 (of class II) antibodies. An anti-Volvox yptl antibody did not show immunoreactivity to the 21 kDa pea protein, although it crossreacted strongly with a 28 kDa pea plumule protein. Our results strongly suggest that the 21 kDa pea protein is an analog of the ARF protein localized in the cytosol of mammalian cells. As far as we are aware, this is the first observation of an ARF protein in plants.