Linked Life Data

6395866

Source:http://linkedlifedata.com/resource/pubmed/id/6395866

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1985-2-22
pubmed:abstractText
The rates of cis to trans interconversion of Glt-(Ala)n-Pro-Phe-4-nitroanilides (n = 1-3) were estimated by means of a two-step process with chymotrypsin as the trans-substrate cleaving activity. By the aid of this system, pig kidney and several other tissues contained demonstrable catalytic activity against the cis to trans interconversion of the proline containing peptides. The active protein fraction was purified 38-fold from pig kidney cortex by ammonium sulfate precipitation and a series of column chromatographic techniques. Activity was detected against the cis to trans interconversion of Glt-Ala-Ala-Pro-Phe-4-nitroanilide to a different extent. No activity was found with Phe-Pro-4-nitroanilide. With respect to the substrate specificity, this enzyme must be classified as a peptidyl-prolyl cis-trans-isomerase. The enzyme was strongly inactivated by p-chloromercuribenzoate, sodium dodecylsulfate, Hg2+- and Cu2+-ions, but was not inhibited by metal chelators, diisopropylphosphorofluoridate and chlorotosylamidophenylbutane. The activity is abolished by incubation with trypsin. The enzyme is heat sensitive at 50 degrees C. The results presented in this paper suggest a new type of enzymes, characterized by catalytic activity against conformational interconversions. The possibility of the location of the enzyme on ribosomal particles is discussed.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0232-766X
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1101-11
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
[Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides].
pubmed:publicationType
Journal Article, English Abstract