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Extraction and partial characterization of non‐histone nuclear proteins of Schistosoma mansoni
Author(s) -
Rabelo Elida M. L.,
Campos Elida G.,
Fantappié Marcelo R.,
Rumjanek Franklin D.
Publication year - 1992
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240490210
Subject(s) - schistosoma mansoni , biology , gene , nuclear protein , histone , microbiology and biotechnology , oligonucleotide , biochemistry , immunology , helminths , schistosomiasis , transcription factor
Abstract 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 HM‐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 32 P‐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.