Source:http://linkedlifedata.com/resource/pubmed/id/13491815
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1958-12-1
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/13491815-12999743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13491815-13144771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13491815-13426234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13491815-14907769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13491815-14955615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13491815-16746816
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pubmed:keyword | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
OM
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pubmed:chemical | |
pubmed:status |
OLDMEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-1295
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
41
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
441-50
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pubmed:dateRevised |
2010-6-22
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pubmed:meshHeading | |
pubmed:year |
1958
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pubmed:articleTitle |
Enzymic dephosphorylation of pepsin and pepsinogen.
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pubmed:publicationType |
Journal Article
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