Literature DB >> 3711193

Design of fluorescent probes for an enzyme on the surface of tumour cells.

F S Steven, M M Griffin, R K Al-Ahmad.   

Abstract

The proteolytic enzyme guanidinobenzoatase is specific for arginyl peptide bonds and is capable of degrading fibronectin. This enzyme is associated with the cell surface of tumour cells in formaldehyde-fixed wax-embedded sections of human pathological tissue. We have designed fluorescent probes for the active site of guanidinobenzoatase: these probes act as competitive inhibitors and can be used to locate cells possessing guanidinobenzoatase. The processes of designing probes, testing their potential as inhibitors, and applying these probes to tumour cell location, all depend upon affinity principles.

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Year:  1986        PMID: 3711193     DOI: 10.1016/s0378-4347(00)80838-5

Source DB:  PubMed          Journal:  J Chromatogr


  3 in total

1.  The synthesis, kinetic characterization and application of biotinylated aminoacylchloromethanes for the detection of chymotrypsin and trypsin-like serine proteinases.

Authors:  G Kay; J R Bailie; I M Halliday; J Nelson; B Walker
Journal:  Biochem J       Date:  1992-04-15       Impact factor: 3.857

2.  The inhibition of a tumour cell surface protease in vivo and its re-activation by oxidation.

Authors:  F S Steven; H Ali; M M Griffin
Journal:  Br J Cancer       Date:  1988-02       Impact factor: 7.640

3.  A study of guanidinobenzoatase during development of mesothelioma induced in the rat by fibrous erionite.

Authors:  F S Steven; R J Hill
Journal:  Br J Cancer       Date:  1988-11       Impact factor: 7.640

  3 in total

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