Linked Life Data

6794986

Source:http://linkedlifedata.com/resource/pubmed/id/6794986

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-1-9
pubmed:abstractText
Circular dichroism and the fluorescent probe, 2-p-toluidinyl-naphthalene-6-sulfonate, were used to compare the molecular properties of pepsin-solubilized vitreous collagen with cartilage and calfskin collagens. Type II vitreous and cartilage collagens have more hydrophobic regions along their molecular domain than does type I calfskin collagen. The rate of fibril growth is faster in type II collagens than in type I. The increased hydrophobicity of type II collagens is attributed to high carbohydrate content and compositional variations. Although the secondary structures of the three collagens do not differ significantly, differences in carbohydrate content, composition, and hydrophobic character may cause some variations in the tertiary structures. It is suggested that the tertiary structure plays an important role in the nature and rate of fibril growth. Differences between cartilage and vitreous collagen in fluorescence behavior, fibril growth, and melting temperature indicate that vitreous collagen may be a "special type II collagen."
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0271-3683
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
175-81
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Spectroscopic studies on pepsin-solubilized vitreous and cartilage collagens.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.