Nanomolar concentrations of Bowman-Birk soybean protease inhibitor suppress x-ray-induced transformation in vitro.
- 1 August 1985
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 82 (16) , 5395-5399
- https://doi.org/10.1073/pnas.82.16.5395
Abstract
Experiments reported here indicate a crude soybean extract, if defatted with acetone, effectively blocks cell transformation in vitro. An active component of this crude extract is the Bowman-Birk trypsin and chymotrypsin inhibitor. The chymotrypsin-inhibitory region of the Bowman-Birk inhibitor is responsible for suppressing in vitro transformation. Another low MW soybean trypsin inhibitor does not significantly suppress transformation. The Bowman-Birk inhibitor has an irreversible effect on the transformation process, can suppress radiation-induced transformation even when added to cultures many days after the carcinogen exposure and is effective in its ability to suppress transformation when present in the medium at a concentration as low as 0.125 nM.This publication has 20 references indexed in Scilit:
- Timing of the steps in transformation of C3H 10T½ cells by X-irradiationNature, 1984
- Inhibition of superoxide production in human neutrophils by purified soybean polypeptides. Re-evaluation of the involvement of proteases.Journal of Biological Chemistry, 1983
- Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts.Proceedings of the National Academy of Sciences, 1983
- Antipain, but not cycloheximide, suppresses radiation transformation when present for only one day at five days post-irradiationCarcinogenesis: Integrative Cancer Research, 1981
- Relationship between x-ray exposure and malignant transformation in C3H 10T1/2 cells.Proceedings of the National Academy of Sciences, 1980
- Protein Inhibitors of ProteinasesAnnual Review of Biochemistry, 1980
- Protease inhibitors suppress radiation-induced malignant transformation in vitroNature, 1978
- Purification, partial characterization, and immunological relationships of multiple low molecular weight protease inhibitors of soybeanBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- A trypsin and chymotrypsin inhibitor from chick peas (Cicer arietinum)Biochemical Journal, 1976
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976