Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-5-11
pubmed:abstractText
The hydrophobic properties of salivary mucus glycoprotein were investigated by fluorescence spectroscopy using bis(8-anilino-1-naphthalene-sulfonate). The mucin, purified from rat submandibular salivary gland, was subjected to removal of associated and covalently bound lipids, degradation with pronase, and reduction with beta-mercaptoethanol, and titrated with the probe. Analyses of fluorescence data revealed the presence of 49 +/- 5 hydrophobic binding sites in the intact mucin molecule, a 69% increase in the number of binding sites occurred following extraction of associated lipids, while the removal of covalently bound fatty acids caused a 25% decrease in the binding sites. Proteolytic destruction of the nonglycosylated regions of the glycoprotein essentially abolished the probe binding, whereas reduction produced glycoprotein subunits whose combined number of hydrophobic binding sites was 2.4 times greater than that of mucus glycoprotein polymer. The results suggest that associated and covalently bound lipids contribute to hydrophobic characteristics of salivary mucin and that the hydrophobic binding sites reside on the nonglycosylated regions of this glycoprotein buried within its core.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
151
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1046-53
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Role of associated and covalently bound lipids in salivary mucin hydrophobicity: effect of proteolysis and disulfide bridge reduction.
pubmed:affiliation
Research Center, School of Dentistry, University of Medicine and Dentistry of New Jersey, Newark 07103-2425.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.