|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0030685,
umls-concept:C0030946,
umls-concept:C0063693,
umls-concept:C0086418,
umls-concept:C0391871,
umls-concept:C0475264,
umls-concept:C0567416,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1963578
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
1985-8-22
|
|
pubmed:abstractText |
The N-terminal amino-acid sequence of human ITI has been found to be identical with that of the acid-stable human 30-kDa inhibitors (HI-30) from urine, serum, and those released from inter-alpha-trypsin inhibitor by trypsin or chymotrypsin. Serum HI-30 and HI-30 released by trypsin differ from the urinary inhibitor by an additional C-terminal arginine residue. Compared to these two inhibitors the inhibitor released by chymotryptic proteolysis is elongated C-terminally by an additional phenylalanine residue. These results strongly favour HI-30 as the N-terminus of the inter-alpha-trypsin inhibitor and its release from this inhibitor in vivo by cleavage of the Arg123-Phe124 peptide bond by trypsin-like proteinases.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0177-3593
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
366
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
479-83
|
|
pubmed:dateRevised |
2004-11-17
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1985
|
|
pubmed:articleTitle |
Human inter-alpha-trypsin inhibitor: localization of the Kunitz-type domains in the N-terminal part of the molecule and their release by a trypsin-like proteinase.
|
|
pubmed:publicationType |
Journal Article
|
