Linked Life Data

2558505

Source:http://linkedlifedata.com/resource/pubmed/id/2558505

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-2-9
pubmed:abstractText
A new and specific tissue kallikrein-binding protein was identified in mammalian serum and in secreted transformed-cell culture media (Chao et al., Biochem. J. 239: 325-331, 1986). We have designated this kallikrein-binding protein as "kallistatin". Human kallistatin has been purified from serum, using chromatographic steps including DEAE-Sephadex, hydroxylapatite, Cibacron blue-Sepharose, Sephacryl S200, and preparative polyacrylamide gel electrophoresis. The purified kallistatin consists of a single polypeptide chain with an apparent molecular weight of approximately 54 kDa and isoelectric point of approximately 5.0. Kallistatin was eluted as a single peak on reverse-phase HPLC. The purified kallistatin and 125I-labelled human tissue kallikrein form a approximately a 92 kDa SDS- and heat-stable complex. The complex formation is pH dependent and is inhibited by 0.1% (W/V) of deoxycholate or SDS but not by 0.5% (W/V) of Triton X-100, digitonin, Lubrol or CHAPS. A approximately 54 kDa protein was identified in partially purified kallistatin by polyclonal anti-kallistatin antibodies in Western blot analysis and by its binding to 125I-labelled-human tissue kallikrein in ligand blotting. The role of kallistatin in regulating tissue kallikrein activity and metabolism may now be evaluated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-2598
pubmed:author
pubmed:issnType
Print
pubmed:volume
247B
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-8
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Human kallistatin, a new tissue kallikrein-binding protein: purification and characterization.
pubmed:affiliation
Department of Pharmacology, Medical University of South Carolina, Charleston 29425.
pubmed:publicationType
Journal Article