Characterization of a thiol proteinase secreted by malignant human breast tumours.
Biochim Biophys Acta
; 614(1): 134-43, 1980 Jul 10.
Article
em En
| MEDLINE
| ID: mdl-6994814
ABSTRACT
It has previously been demonstrated (Poole, A.R., Tiltman, K.J., Recklies, A.D. and Stoker, T.A.M. (1978) Nature 273, 545-547) that malignant human breast tumours maintained in organ culture secrete elevated amounts of a thiol proteinase. This enzyme has been shown to possess enzymic properties similar to those of cathepsin B (EC 3.4.22.1) with respect to specificity, affinity and pH optima for synthetic substrates. However, the tumour enzyme is much more stable than human liver cathepsin B to inactivation above neutral pH, and it also has a large molecular size and a more acidic isoenzyme pattern. The stability of this enzyme under physiological conditions may allow it to play a role in tumour invasion and metastasis.
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Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Neoplasias da Mama
Limite:
Female
/
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1980
Tipo de documento:
Article