| Literature DB >> 6994814 |
J S Mort, A D Recklies, A R Poole.
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.Entities:
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Year: 1980 PMID： 6994814 DOI： 10.1016/0005-2744(80)90174-6
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002