Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-5-7
pubmed:abstractText
The putative inhibitor domain of Alzheimer's disease amyloid protein precursor was purified from E. coli containing a synthetic gene encoding the Kunitz domain. The purified protein (A4 inhibitor) inhibited the activity of trypsin, forming a 1:1 molar complex with the enzyme. It also strongly inhibited plasmin (Ki = 7.5 x 10(-11) M) from human serum and tryptase (Ki = 2.2 x 10(-10) M) from rat mast cells (tryptase M). In addition, it inhibited rat pancreatic trypsin, alpha-chymotrypsin and kallikrein and human serum kallikrein, but did not inhibit rat chymase, pancreatic elastase, alpha-thrombin, urokinase, papain or cathepsin B.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
167
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
716-21
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:1969731-Amino Acid Sequence, pubmed-meshheading:1969731-Amyloid, pubmed-meshheading:1969731-Amyloid beta-Protein Precursor, pubmed-meshheading:1969731-Animals, pubmed-meshheading:1969731-Cloning, Molecular, pubmed-meshheading:1969731-Escherichia coli, pubmed-meshheading:1969731-Fibrinolysin, pubmed-meshheading:1969731-Genes, Synthetic, pubmed-meshheading:1969731-Humans, pubmed-meshheading:1969731-Kinetics, pubmed-meshheading:1969731-Mast Cells, pubmed-meshheading:1969731-Molecular Sequence Data, pubmed-meshheading:1969731-Peptide Hydrolases, pubmed-meshheading:1969731-Protein Precursors, pubmed-meshheading:1969731-Rats, pubmed-meshheading:1969731-Substrate Specificity, pubmed-meshheading:1969731-Trypsin, pubmed-meshheading:1969731-Trypsin Inhibitor, Kunitz Soybean, pubmed-meshheading:1969731-Trypsin Inhibitors
pubmed:year
1990
pubmed:articleTitle
Protease-specificity of Kunitz inhibitor domain of Alzheimer's disease amyloid protein precursor.
pubmed:affiliation
Division of Enzyme Chemistry, University of Tokushima, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't