Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-6-4
pubmed:abstractText
The alpha 1 alpha 2 alpha 3-chain form of human type V collagen was solubilized from placenta by pepsin treatment and isolated by ion-exchange chromatography. The alpha 3-chain was further separated after denaturation of the triple helix also by ion-exchange chromatography, cleaved with lysyl endopeptidase and the fragments separated by size-exclusion chromatography and reversed phase HPLC. N-Terminal sequence analysis of the fragments and comparison to sequences contained in a database indicated a relatively high similarity of the alpha 3(V)-chain to alpha 1(V) and alpha 1(XI) with an identity of approximately 73%.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
373
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-75
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing.
pubmed:affiliation
Max-Planck-Institut für Biochemie, Martinsried, Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't