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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-2-9
pubmed:abstractText
Human pancreatic kallikrein (H.Panc.K.) was purified from human pancreas by ion exchange chromatography on DEAE-cellulose, affinity chromatographies on p-aminobenzamidine Sepharose 6B and aprotinin aminocellulofine, followed by gel filtration on Sephacryl S-200. The final preparation had a specific activity of 9.2 AU/A280 (AU; amidase unit for H-Pro-Phe-Arg-MCA) and its N-terminal sequence coincided with the reported sequence for H.Panc.K.. In HPLC (gel filtration), one symmetrical peak corresponding to a molecular weight of 48,000 was obtained. In SDS-PAGE without 2-mercaptoethanol (2-ME), one band corresponding to a molecular weight of 52,000 was obtained, but with 2-ME, 2 bands, 52,000 and 30,000, were obtained. Km value for MCA was 4.9 x 10(-2) mM. Proteinase inhibitor specificities of H.Panc.K. were the same as those of human urinary kallikrein (HUK) and hog pancreatic kallikrein (hog Panc.K.), while anti-HUK antibody inhibited the activities of H.Panc.K. and HUK, but not that of hog Panc.K.. From the analysis of affinity for concanavalin A (Con A) and erythroagglutinating phytohemagglutinin (E-PHA), the carbohydrate parts of H.Panc.K. are relatively rich in biantennary complex type sugar chains with bisecting GlcNAc compared with those of human salivary kallikrein (H.Saliv.K.) and HUK.
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
177-82
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Characterization of human pancreatic kallikrein.
pubmed:affiliation
1st Department of Surgery, Faculty of Medicine, University of Tokyo, Japan.
pubmed:publicationType
Journal Article