Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1958-12-1
pubmed:abstractText
It has been shown by the work presented in this paper that it is possible to dephosphorylate enzymically pepsin and pepsinogen with a variety of phosphatases. With the aid of a phosphodiesterase and the prostate phosphatase it has been established that the phosphorus in the two proteins is present as a diester and connects two sites of the peptide chain in a cyclic configuration. Removal of the phosphorus does not affect the proteolytic activity against hemoglobin or the synthetic substrate acetyl-L-phenylalanyl diiodotryosine, nor the pepsinogen pepsin transformation. However, an increase of the autodigestion of pepsin is observed.
pubmed:commentsCorrections
pubmed:keyword
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
OM
pubmed:chemical
pubmed:status
OLDMEDLINE
pubmed:month
Jan
pubmed:issn
0022-1295
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
441-50
pubmed:dateRevised
2010-6-22
pubmed:meshHeading
pubmed:year
1958
pubmed:articleTitle
Enzymic dephosphorylation of pepsin and pepsinogen.
pubmed:publicationType
Journal Article