Linked Life Data

2460093

Source:http://linkedlifedata.com/resource/pubmed/id/2460093

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-11-14
pubmed:abstractText
Pancreatic juice collected by endoscopic retrograde cannulation of the pancreatic duct after administration of secretin and pancreozymin was analyzed by pore gradient polyacrylamide gel electrophoresis. Two electrophoretic systems, an alkaline (pH 8.9) and an acidic (pH 5.0), were elaborated to obtain optimal separation of exocrine proteins. 13 bands under alkaline conditions and 17 bands by running in the acidic system were separated and distinguished by Coomassie-Brilliant Blue G 250 staining. Fourteen proteins were identified using enzymatic and immunological methods: one form of each of lipase, chymotrypsinogen, prophospholipase A2, procarboxypeptidase A and trypsin inhibitor, two forms of each of procarboxypeptidase B and proelastase, three forms of each of trypsinogen and amylase. An additional band was identified as albumin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0232-766X
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-40
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Analysis of human exocrine pancreatic proteins by means of pore gradient polyacrylamide gel electrophoresis.
pubmed:affiliation
Institute of Policlinical Medicine, Karl Marx University Leipzig, GDR.
pubmed:publicationType
Journal Article