Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1990-9-4
pubmed:abstractText
A high molecular-weight mucin was purified from human submandibular-sublingual saliva. The purity of the mucin preparation was demonstrated by the absence of other salivary proteins, by antibody reactivity and by gel electrophoresis. After reduction with mercaptoethanol a putative link component with approximate Mr 150,000 and a glycoprotein component of higher Mr could be detected by gel electrophoresis. These subunits were subsequently purified and they showed distinct differences in their amino acid compositions, demonstrating that the mucin consisted of two different subunits. The link had a number of similarities with the link component of intestinal mucin and a parotid agglutinin and has previously been shown to cross-react with antiserum to link component from intestinal mucin. Salivary and intestinal mucins may therefore have similar subunit structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0003-9969
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
265-72
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Purification and characterization of subunits of a high molecular weight human salivary mucin.
pubmed:affiliation
Department of Biochemistry, University of Toronto, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't