Cell-surface and secreted proteinases and guanidinobenzoatase activity.
Hydrolysis of p-nitrophenyl guanidinobenzoate is characteristic of a tumour cell surface proteinase. We found this activity in three transformed or tumour cell lines, but not in two normal fibroblast strains. Immunochemical inhibition of plasminogen activator activity did not affect guanidinobenzoatase activity.
Perry
J K
JK
Department of Biochemistry, University of Auckland, New Zealand.
Scott
G K
GK
D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000032:analysis*; D002461:Cell Line, Transformed; D010450:Endopeptidases; D006367:HeLa Cells; D006801:Humans; D006868:Hydrolysis; D007739:L Cells; D051379:Mice; D010960:Plasminogen Activators / Q000032:analysis* / Q000096:biosynthesis; D010959:Tissue Plasminogen Activator / Q000032:analysis* / Q000096:biosynthesis; D015291:Transforming Growth Factors / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D015291:Transforming Growth Factors; D002265:Carboxylic Ester Hydrolases; C037288:guanidinobenzoate esterase; D010450:Endopeptidases; D010960:Plasminogen Activators; D010959:Tissue Plasminogen Activator