Linked Life Data

868635

Source:http://linkedlifedata.com/resource/pubmed/id/868635

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1977-7-23
pubmed:abstractText
During the purification of propancreatopeptidase E, a proATEEase activity is always copurified. The proelastolytic and proesterolytic activities can be separated on a hydroxylapatite column. The zymogen with potential ATEEase activity has a basic isoelectric point, can be activated by trypsin, and can hydrolyse elastin and ATEE but not ATAME. Its molecular weight is about 26,500 and the NH2-terminal sequence indicates clearly that it belongs to the chymotrypsinogen family, but that it is not chymotrypsinogen A, B, or C. We call it chymotrypsinogen D. Although both pancreatopeptidase E and chymotrypsin D can hydrolyse elastin, the synthetic substrate ATAME is attacked only by pancreatopeptidase E. Therefore, the peptide bonds in elastin cleaved by these two enzymes should be different.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-2598
pubmed:author
pubmed:issnType
Print
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-75
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Chymotrypsinogen D, a new zymogen from porcine pancreas with proelastolytic activity.
pubmed:publicationType
Journal Article