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Extraction and partial characterization of non-histone nuclear proteins of Schistosoma mansoni

✍ Scribed by Elida M. L. Rabelo; Elida G. Campos; Marcelo R. Fantappié; Franklin D. Rumjanek

Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
738 KB
Volume
49
Category
Article
ISSN
0730-2312

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✦ Synopsis

A pool of nuclear proteins from adult worms of Schistosorna rnansoni was analyzed for amino acid cornposition and found to be compatible with high mobility group (HMG) proteins. One of the schistosome HMG proteins was identified as HMG 2 by one-dimensional and two-dimensional PAGE. Stage-specific differences in the HMG-like protein composition were encountered when adult worms were compared to schistosomula, the larval form. Immobilization of the adult male and female nuclear proteins onto nitrocellulose, followed by hybridization against 3zP-F-10, a schistosome sex specific gene encoding a major egg shell protein, revealed distinct banding patterns. On the other hand, a synthetic oligonucleotide, derived from the 3'untranslated end of the F-I 0 gene and possibly containing one regulatory element of the gene, bound mainly to male low MW proteins.

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