Extraction and partial characterization of non-histone nuclear proteins of Schistosoma mansoni.
A pool of nuclear proteins from adult worms of Schistosoma mansoni was analyzed for amino acid composition 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 32P-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-10 gene and possibly containing one regulatory element of the gene, bound mainly to male low MW proteins.
Rabelo
E M
EM
Department of Developmental Biochemistry, National Institute for Medical Research, London, England.
Campos
E G
EG
Fantappié
M R
MR
Rumjanek
F D
FD
D000375:Aging; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001483:Base Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification; D005260:Female; D006609:High Mobility Group Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008297:Male; D008969:Molecular Sequence Data; D012550:Schistosoma mansoni / Q000737:chemistry*
D000596:Amino Acids; D004268:DNA-Binding Proteins; D006609:High Mobility Group Proteins