Molecular and biochemical studies of Trichomonas vaginalis.

Molecular and biochemical studies of Trichomonas vaginalis.

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Title: Molecular and biochemical studies of Trichomonas vaginalis.
Author: Petrin, Dino P.
Abstract: Trichomonas vaginalis is known to produce a 60 kDa extracellular cysteine proteinase (ECP) that is believed to be important in the initial stages of T. vaginalis infection. Upon further purification, the 60 kDs protein breaks down into a 43 and 23 kDa subunits. Anti-serum raised against a purified preparation of the 23 kDa subunit was used to screen a $\lambda$ gt11 T. vaginalis cDNA library. The strongest reactive clone of the four was partially sequenced and found to have homology to an exoantigen called ABRA found in Plasmodium falciparum. It was decided to sequence the other three clones to determine if they contained sequences that are indicative of cysteine proteinases (CP). Molecular analysis of the remaining clones indicated that they were distinct and did not represent cysteine proteinases. By using the cDNA sequence of 23-4-2, gene specific primers (GSPs) were used in RACE PCR in an effort to obtain a translational start codon and to determine if the putative gene designated bdh was polyadenylated. To determine if T. vaginalis did produce butanol as a byproduct of metabolism, T. vaginalis cultures were incubated under anaerobic conditions and subsequently under aerobic and anaerobic conditions and the culture supernatants were extracted with ether. (Abstract shortened by UMI.)
Date: 1997
URI: http://hdl.handle.net/10393/4451

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