Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1981-3-24
pubmed:abstractText
Exocrine proteins contained in human pancreatic juice were separated in two dimensions using isoelectric focusing and sodium dodecyl sulfate gel electrophoresis. Nineteen discrete proteins were found. Fifteen of these were identified by actual or potential enzyme activity and include three forms of trypsinogen, two forms each of procarboxypeptidase A, procarboxypeptidase B, proelastase, and colipase, and one form each for amylase, lipase, chymotrypsinogen, and prophospholipase A2. Lipase and four unidentified proteins were found to contain carbohydrate by the periodic acid Schiff staining method. Each pancreatic protein was characterized by isoelectric point and molecular weight. Proteins were quantitated according to relative mass, as measured by the incorporation of a mixture of 15 3H-amino acids into secretory proteins contained in tissue slices, and according to the distribution of Coomassie blue R stain among proteins contained in pancreatic juice, as determined by two-dimensional gel scanning and computer analysis. The second form of pancreatic procarboxypeptidase B (IEPn6.7) was present in only 4 of 10 subjects tested. Trypsinogens 1 and 3 were covalently labeled with 35SO4. Trypsin derived from trypsinogen 2 showed no inhibition with soybean trypsin inhibitor or Trasylol.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0016-5085
pubmed:author
pubmed:issnType
Print
pubmed:volume
80
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
461-73
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Characterization of human exocrine pancreatic proteins by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't