REVERSIBLE DISSOCIATION OF A TUMOR-CELL SURFACE PROTEASE-INHIBITOR COMPLEX

  • Authors:
    • FS STEVEN
    • MM GRIFFIN
    • DC BLAKEY
  • View Affiliations

  • Published online on: June 1, 1992     https://doi.org/10.3892/ijo.1.1.59
  • Pages: 59-61
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Abstract

Tumour cell surfaces possess a cell surface protease (GB), which can be recognised by a cytoplasmic inhibitor protein prepared from cultured tumour cells. This enzyme inhibitor complex has been shown to be reversibly dissociated by 10-(4)M sodium dodecyl sulphate. Sections of frozen tumour tissue were used to provide cells with active GB and the successful recognition and inhibition of this GB was followed by fluorescence microscopy employing the competitive inhibitor 9-amino acridine as a fluorescent probe.

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June 1992
Volume 1 Issue 1

Print ISSN: 1019-6439
Online ISSN:1791-2423

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Spandidos Publications style
STEVEN F, GRIFFIN M and BLAKEY D: REVERSIBLE DISSOCIATION OF A TUMOR-CELL SURFACE PROTEASE-INHIBITOR COMPLEX. Int J Oncol 1: 59-61, 1992
APA
STEVEN, F., GRIFFIN, M., & BLAKEY, D. (1992). REVERSIBLE DISSOCIATION OF A TUMOR-CELL SURFACE PROTEASE-INHIBITOR COMPLEX. International Journal of Oncology, 1, 59-61. https://doi.org/10.3892/ijo.1.1.59
MLA
STEVEN, F., GRIFFIN, M., BLAKEY, D."REVERSIBLE DISSOCIATION OF A TUMOR-CELL SURFACE PROTEASE-INHIBITOR COMPLEX". International Journal of Oncology 1.1 (1992): 59-61.
Chicago
STEVEN, F., GRIFFIN, M., BLAKEY, D."REVERSIBLE DISSOCIATION OF A TUMOR-CELL SURFACE PROTEASE-INHIBITOR COMPLEX". International Journal of Oncology 1, no. 1 (1992): 59-61. https://doi.org/10.3892/ijo.1.1.59