rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1991-2-12
|
pubmed:abstractText |
The human blood protein pre-alpha-inhibitor is composed of one heavy and one light protein chain. The chains are covalently linked to each other by a structure that has not previously been described, which we designate a protein-glycosaminoglycan-protein (PGP) cross-link. A combination of protein and carbohydrate analytical techniques indicates that the interchain linkage is mediated by a chondroitin 4-sulfate glycosaminoglycan that originates from a typical O-glycosidic link to Ser-10 of the light chain. The heavy chain is esterified, via the alpha-carbon of its C-terminal Asp, to C-6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain. This PGP cross-link may be present in other proteins, but could have been overlooked due to the heterogeneous behavior of proteins containing glycosaminoglycan.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
266
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
747-51
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:1898736-Amino Acids,
pubmed-meshheading:1898736-Blood Proteins,
pubmed-meshheading:1898736-Blotting, Western,
pubmed-meshheading:1898736-Carbohydrates,
pubmed-meshheading:1898736-Chondroitin Sulfates,
pubmed-meshheading:1898736-Cross-Linking Reagents,
pubmed-meshheading:1898736-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1898736-Glycosylation,
pubmed-meshheading:1898736-Humans,
pubmed-meshheading:1898736-Mass Spectrometry,
pubmed-meshheading:1898736-Protein Precursors,
pubmed-meshheading:1898736-Trypsin Inhibitors
|
pubmed:year |
1991
|
pubmed:articleTitle |
Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor.
|
pubmed:affiliation |
Department of Pathology, Duke University Medical Center, Durham, North Carolina 27710.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|