Linked Life Data

17604201

Source:http://linkedlifedata.com/resource/pubmed/id/17604201

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-8-6
pubmed:databankReference
pubmed:abstractText
The organic fraction of epiphragm mucus from the snail Cernuella virgata (Mollusca: Helicidae) consists predominantly of protein (17-23 dry wt.%) rather than carbohydrate (< or =0.4-2.0 dry wt.%), and the former underpins epiphragm membrane structure. The major protein ('epiphragmin') has an apparent molecular mass of approximately 86 kDa and is encoded by a cDNA (Genbank accession EF602752) which specifies a secreted protein of 81.2 kDa. The central region of the epiphragmin polypeptide is a coiled coil-forming region which is homologous to part of AglZ, a bacterial filament-forming protein. Coiled coil-driven self-assembly of epiphragmin probably underpins the formation of sheets in epiphragm membranes and the ability of epiphragm mucus to serve as an adhesive. The C-terminal region of epiphragmin is a fibrinogen-related domain (FReD) that is homologous to the fibrinogen-related proteins (FREPs) found in the hemolymph of freshwater snails. The material properties of epiphragm membranes resemble those of bovine ligament elastin. Wooden lap-joints bonded by rehydrated epiphragm fragments developed dry shear strength values of 1.4+/- 0.1 MPa.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1096-4959
pubmed:author
pubmed:issnType
Print
pubmed:volume
148
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
192-200
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Epiphragmin, the major protein of epiphragm mucus from the vineyard snail, Cernuella virgata.
pubmed:affiliation
CSIRO Molecular & Health Technologies, Sydney Laboratory, P.O.Box 184, North Ryde, NSW 1670, Australia.
pubmed:publicationType
Journal Article