Linked Life Data

7275004

Source:http://linkedlifedata.com/resource/pubmed/id/7275004

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1981-11-18
pubmed:abstractText
The synthesis of 5-carboxyvaleryl- and 3-carboxypropionyl-L-phenylalanine beta-naphthyl ester (Adi-Phe-ONap, Suc-Phe-ONap) and 3-carboxypropionyl-L-phenylalanine p-nitrophenyl ester (Suc-Phe-ONp) is reported. The two latter compounds were obtained in good yields by 3-carboxypropionylation of the L-phenylalanine aryl esters with succinic anhydride at pH values below 6 in aqueous organic solutions. The beta-naphthyl esters in particular proved to be sensitive substrates for cathepsin G and chymotrypsin. They are not or only slightly hydrolyzed by other proteinases like elastases, kininogenases, e.g. kallikrein, plasmin, thrombin and trypsin. The spontaneous hydrolysis of the beta-naphthyl esters is relatively slow below pH 8. beta-Naphthol split-off during the enzyme reaction may be conveniently monitored at 328.5 nm (epsilon = 1730M-1 X cm-1) or with an at least 15-fold increase in sensitivity in a discontinuous assay after coupling with Fast Garnet at 520 nm (epsilon = 34800M-1 X cm-1). The increase in absorbance is linear with time and proportional to the amount of enzyme up to A 328.5 of at least 0.62. Adi-Phe-ONap is preferentially used for cathepsin G (at 328.5 nm 9.2-fold more sensitive than benzoyl-L-tyrosine ethyl ester, Bz-Tyr-OEt) whereas for chymotrypsin Suc-Phe-ONap is more advantageous (4.2-fold increase in sensitivity at 328.5 nm over Bz-Tyr-OEt). The influence of dimethyl sulphoxide and Brij 35 on the activity of cathepsin G and chymotrypsin was investigated using Suc-Phe-ONap as the substrate. The values of Km and kcat were determined for both enzymes and substrates. Because of the relatively high rates of spontaneous hydrolysis above pH 7.0 the use of Suc-Phe-ONp is less advantageous.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0018-4888
pubmed:author
pubmed:issnType
Print
pubmed:volume
362
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
655-64
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
[Synthesis of omega-carboxyacyl-L-phenylalanine-aryl esters and their use as substrates for cathepsin G and chymotrypsin].
pubmed:publicationType
Journal Article, English Abstract