Linked Life Data

8360170

Source:http://linkedlifedata.com/resource/pubmed/id/8360170

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1993-9-30
pubmed:abstractText
The highly glycosylated domains of rat small intestinal mucins were isolated after reduction and trypsin digestion and separated into two populations (A and B) by gel chromatography. The molecular mass values were 650 and 335 kDa, respectively, and the relative yields suggest that the two glycopeptides occur in equimolar proportions. Electron microscopy revealed linear structures with weight average lengths of 230 nm (A) and 110 nm (B) corresponding to a mass/unit length of about 3 kDa/nm. The protein cores (17-19%) contain large amounts of threonine (over 40%), serine (17-24%), and proline (18-19%). Carbohydrate and sulfate account for approximately 80 and 0.5%, respectively, and gas chromatography-mass spectrometry showed that the patterns of neutral and sialic acid-containing glycans are very similar in the two glycopeptides. Both contain a significant amount (7-10 mol %) of single GalNAc residues, the average oligosaccharide is about 4 sugar residues long, and the largest species observed are heptasaccharides. The major neutral and sialic acid-containing oligosaccharides are Fuc1-2Gal1-3GalNAcol and GlcNAc1-6(NeuGc2-Gal1-3)GalNAcol, respectively. Sialic acid is present as both N-acetyl- and N-glycoloyl-neuraminic acid. Repeated extractions of the tissue with guanidinium chloride left approximately 80% of the mucus glycoproteins as an insoluble glycoprotein complex whereas exposure to dithiothreitol or high speed homogenization accomplished complete solubilization. The "subunits" obtained after reduction with dithiothreitol are larger than glycopeptides A and B, and fragments corresponding in size to the latter are obtained after cleavage with trypsin. Most of the mucins from rat small intestine thus occurs as an insoluble glycoprotein complex composed of subunits joined with disulfide bonds. The subunits contain two highly glycosylated regions with different lengths substituted with very similar oligosaccharides.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18771-81
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed-meshheading:8360170-Amino Acids, pubmed-meshheading:8360170-Animals, pubmed-meshheading:8360170-Binding Sites, pubmed-meshheading:8360170-Carbohydrate Sequence, pubmed-meshheading:8360170-Centrifugation, Isopycnic, pubmed-meshheading:8360170-Glycopeptides, pubmed-meshheading:8360170-Glycosylation, pubmed-meshheading:8360170-Guanidine, pubmed-meshheading:8360170-Guanidines, pubmed-meshheading:8360170-Intestinal Mucosa, pubmed-meshheading:8360170-Intestine, Small, pubmed-meshheading:8360170-Microscopy, Electron, pubmed-meshheading:8360170-Molecular Sequence Data, pubmed-meshheading:8360170-Molecular Weight, pubmed-meshheading:8360170-Mucins, pubmed-meshheading:8360170-N-Acetylneuraminic Acid, pubmed-meshheading:8360170-Oligosaccharides, pubmed-meshheading:8360170-Rats, pubmed-meshheading:8360170-Rats, Sprague-Dawley, pubmed-meshheading:8360170-Sialic Acids
pubmed:year
1993
pubmed:articleTitle
Characterization of two different glycosylated domains from the insoluble mucin complex of rat small intestine.
pubmed:affiliation
Department of Physiological Chemistry 2, University of Lund, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't