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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1991-2-13
|
pubmed:abstractText |
The substitution of aspartic acid for the naturally-occurring histidine residue in position B10 in human insulin results in an insulin analogue which displays an in vitro potency 4- to 5-fold greater than the parent compound. This substitution has been introduced into six insulin analogues which, before modification, display potencies ranging from less than 0.01-fold to 3-fold relative to natural insulin. In each case, the resulting aspartic acid-substituted analogue is substantially more potent than the parent compound. Thus, it is now possible to prepare "tailor-made" insulins with enhanced potency.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
31
|
pubmed:volume |
173
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
982-7
|
pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading | |
pubmed:year |
1990
|
pubmed:articleTitle |
Superactive insulins.
|
pubmed:affiliation |
Department of Biochemistry, Mount Sinai School of Medicine, City University of New York, New York 10029-6574.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|