Linked Life Data

738700

Source:http://linkedlifedata.com/resource/pubmed/id/738700

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1979-4-25
pubmed:abstractText
Ac-Phe-ArgOMe is hydrolyzed much faster than are Bz-ArgOEt, Z-ArgOMe, or Ac-Gly-ArgOMe by the kallikrein from human urine. The synthesis of Ac-Phe-ArgOEt is described. Hydrolysis of this substrate can be conveniently monitored by a coupled spectrophotometric procedure. Increase in absorbance is linear with time and proportional to the amount of kallikrein up to a deltaA366 of at least 0.22/10 min. This assay for human urinary kallikrein is 46-fold more sensitive than that based on Bz-ArgOEt and 38-fold more sensitive than that with D-Val-Leu-Arg-p-nitroanilide. A number of other arginine p-nitroanilides are hydrolyzed by this enzyme at still lower rates. The assay of human urinary kallikrein with D-Val-Leu-ArgOEt is about a factor of two less sensitive than the assay with Ac-Phe-ArgOEt. This also holds for Z-TyrONp, which displays a rapid spontaneous hydrolysis. Furthermore, the rate of the enzymic reaction with Z-TyrONp drops off rapidly.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0018-4888
pubmed:author
pubmed:issnType
Print
pubmed:volume
359
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1667-73
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Peptide esters and nitroanilides as substrates for the assay of human urinary kallikrein.
pubmed:publicationType
Journal Article