Linked Life Data

889800

Source:http://linkedlifedata.com/resource/pubmed/id/889800

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1977-10-14
pubmed:abstractText
Enterokinase has been isolated from the contents of bovine duodena and purified 1200-fold in 41% yield. The isolation procedure employed DEAE chromatography, affinity chromatography on immobilized p-aminobenzamidine, and gel filtration. The resultant pure enzyme exhibits a single band on sodium dodecyl sulfate gel electrophoresis corresponding to a molecular weight of 145 000. Two chains in the molecule, connected by disulfide linkages, have molecular weights of 57 000 and 82 000, respectively. The purified enzyme exhibits a restricted specificity which is directed toward the polyanionic amino acid sequence in the activation peptide of the zymogen substrate. Of the zymogens of the serine proteases tested, including several of those involved in blood coagulation, only native and guanidinated trypsinogen are acitvated by enterokinase, whereas acetylated trypsinogen is not. Partial heat denaturation of bovine enterokinase causes a differential response toward the activation of trypsinogen and the hydrolysis of benzoyl-L-arginine ethyl ester (BZArgOEt), further suggesting that secondary sites are important in the binding of trypsinogen. A sensitive assay for enterokinase (nanomole range) was developed using tritiated BZArgOEt.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3354-60
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Bovine enterokinase. Purification, specificity, and some molecular properties.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.