|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1983-6-23
|
|
pubmed:abstractText |
The effect of chemical modification of arginine and lysine residues of fibronectin on its antigenic and gelatin-binding activity was studied by enzyme immunoassay techniques. Both modifications strongly reduced the gelatin-binding activity. Using conformation-specific antibodies it was shown that modification of lysines caused extensive conformational changes in the molecule. No such changes could be detected in arginine-modified fibronectin. The results suggest that arginine residues are directly involved in the binding of fibronectin to gelatin. Lysine residues seem to be important for maintaining a native conformation necessary for gelatin-binding.
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|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0161-5890
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
20
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
149-53
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1983
|
|
pubmed:articleTitle |
Effect of chemical modification of arginine and lysine residues of fibronectin on its antigenic and gelatin-binding activity.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
