Linked Life Data

16520868

Source:http://linkedlifedata.com/resource/pubmed/id/16520868

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-3-7
pubmed:abstractText
A convenient and rapid method for the photo-regulation of the proteolytic enzyme alpha-chymotrypsin is described. When alpha-chymotrypsin is coated with photolytic 1-(2-nitrophenyl)ethanol residues this not only markedly reduces the capability of the enzyme to digest both of the small substrates N-benzoyl-L-tyrosine ethyl ester and N-succinyl-L-phenylalanine p-nitroanilide, but also completely inhibits the enzyme's proteolytic activity. The inactivated alpha-chymotrypsin can then be reactivated under physiological conditions, when and where it is required, by exposure to UV-A light. These results further demonstrate that 1-(2-nitrophenyl)ethanol coated proteins can often be used as light sensitive biological switches as a simple alternative to site directed procedures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1474-905X
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
326-30
pubmed:dateRevised
2009-1-8
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
A simple procedure for the photoregulation of chymotrypsin activity.
pubmed:affiliation
Diagnostic and Therapeutic Technologies, School of Clinical and Laboratory Sciences, University of Newcastle upon Tyne, The Medical School, Newcastle upon Tyne, NE2 4HH, UK. C.H.Self@ncl.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't