Linked Life Data

7958421

Source:http://linkedlifedata.com/resource/pubmed/id/7958421

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-11-29
pubmed:databankReference
pubmed:abstractText
A 32-kDa protein (HLC-32) was purified from sea urchin embryos and characterized. In indirect immunofluorescence analysis this species was found to be distributed throughout the cytoplasm of the unfertilized egg but within 1 hr following fertilization was localized to the hyaline layer with some residual immunofluorescence remaining within the cytoplasm of the single cell embryo. By the early blastula stage the antigen was also detected in the basal lamina, indicating a bidirectional transport mode for this protein. A cDNA clone was isolated from a lambda Zap expression library. Sequence analysis revealed a protein rich in acidic (12.4 mole%) and basic (14.3 mole%) residues. Comparative sequence analysis revealed 41 and 47% amino acid sequence homology with two butanol-extractable proteins previously isolated from blastula stage embryos of the sea urchin Paracentrotus lividus. DNA gel blot analysis indicated that the gene encoding HLC-32 belonged to a small multigenic family, while in RNA gel blot analyses a 1.4-kB transcript was detected in ovaries but not gut, testes, mature eggs, or various stage embryos. At the early blastula stage of development this protein underwent a post-translational modification reaction which resulted in the loss of a 4-amino-acid peptide fragment from the amino-terminal end of this species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0012-1606
pubmed:author
pubmed:issnType
Print
pubmed:volume
165
pubmed:geneSymbol
HLC-32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
556-65
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Cloning and characterization of HLC-32, a 32-kDa protein component of the sea urchin extraembryonic matrix, the hyaline layer.
pubmed:affiliation
Department of Biochemistry, Memorial University of Newfoundland, St. John's, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't