|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0007004,
umls-concept:C0008551,
umls-concept:C0063693,
umls-concept:C0077906,
umls-concept:C0086418,
umls-concept:C0205409,
umls-concept:C0439801,
umls-concept:C0597304,
umls-concept:C1441547,
umls-concept:C1947905,
umls-concept:C1961133,
umls-concept:C1999228,
umls-concept:C2673177
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|
pubmed:issue |
10
|
|
pubmed:dateCreated |
1982-2-12
|
|
pubmed:abstractText |
The inhibitory active part of the inter-alpha-trypsin inhibitor with a known amino acid sequence is present as an acid-resistant inhibitor in human serum, in urine, in bronchial and in nasal mucus. The inhibitor molecule has a 50% carbohydrate content. Carbohydrate side chains are attached in two positions. One chain is linked to the polypeptide O-glycosidically via the serine residue in position 10 in the N-terminal extension peptide. The second side chain is attached N-glycosidically via the asparagine residue in position 24, located in the inactive "inhibitory" Kunitz-type domain of the inhibitor. The composition of the carbohydrate side chains were determined.
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|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0018-4888
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
362
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1357-62
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1981
|
|
pubmed:articleTitle |
Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, V. Attachments of carbohydrates in the human urinary trypsin inhibitor isolated by affinity chromatography.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
