Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-8-20
pubmed:abstractText
Rat tail tendon collagen can be solubilized by a neutral aqueous solution containing 2% Tris dodecyl sulfate at 4 degrees C without being unfolded to its constituent polypeptides. The solvent at this temperature is particularly suited for gel chromatographic separation of native collagen. Thus Sepharose CL-2B gel chromatography was found to separate the monomeric collagen molecule from the products of intermolecular cross-linking. The procedure can be effectively used to follow progress of intermolecular cross-linking with aging. The monomeric collagen can be subsequently applied to polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate to evaluate the mode of intramolecular cross-linking.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0174-173X
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
149-56
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Separation of cross-linked products of rat tail tendon collagen from monomeric components by gel chromatography in the presence of Tris dodecyl sulfate at 4 degrees C.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't