Abstract:
:A group of proteins judged on several criteria to be yolk proteins have been isolated from a homogenate of the nematode Caenorhabditis elegans. Comparison of partial proteolysis fragments indicates that the two bands of a 170,000-dalton doublet (yp170) are closely related; bands observed at 115,000 daltons (yp115) and 88,000 daltons (yp88) appear to be structurally distinct. All three yolk protein species are glycoproteins, as judged by binding of the lectin concanavalin A. The yp170 doublet has been purified by gel filtration in the presence of sodium dodecyl sulfate. An antiserum obtained by immunization with the purified yp170 doublet does not bind either of the two smaller proteins. Staining of C. elegans eggs by indirect immunofluorescence with the anti-yp170 serum indicates a dispersed cytoplasmic location for the antigen throughout embryogenesis, with apparent segregation to the intestine immediately prior to hatching.
journal_name
Dev Bioljournal_title
Developmental biologyauthors
Sharrock WJdoi
10.1016/0012-1606(83)90321-4subject
Has Abstractpub_date
1983-03-01 00:00:00pages
182-8issue
1eissn
0012-1606issn
1095-564Xpii
0012-1606(83)90321-4journal_volume
96pub_type
杂志文章abstract::Myf5 is a key myogenic determination factor, specifically present at sites of myogenesis. Surprisingly, during mouse development, this gene is also transcribed in restricted areas of the central nervous system, although the Myf5 protein is not detectable. We have investigated the regulation of Myf5 expression in the c...
journal_title:Developmental biology
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journal_title:Developmental biology
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journal_title:Developmental biology
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journal_title:Developmental biology
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