Inhibition properties of Sepharose-bound trypsin and a protease on the surface of Ehrlich ascites tumour cells
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Elsevier BV
Reference17 articles.
1. Evidence for the Inhibition of Trypsin by Thiols. The Mechanism of Enzyme-Inhibitor Complex Formation
2. The interactiion of a trypsin-dependent neutral protease and its inhibitor found in tumour cells Analysis of complex kinetic data involved in a thiol-disulphide exchange mechanism
3. Properties of Dipeptidyl Arylamidase I of the Pituitary
4. The Hydrolysis of Carbobenzoxy-l-tyrosine p-Nitrophenyl Ester by Various Enzymes
5. Regulation of uracil utilization for RNA synthesis in Ehrlich ascites tumour cells by glucose metabolism
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1. Immobilization of Enzymes: An Approach to Fundamental Studies in Biochemistry;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
2. Further Inhibition Studies on Guanidinobenzoatase, a Trypsin-Like Enzyme Associated with Tumour Cells;Journal of Enzyme Inhibition;1987-01
3. Partial purification and characterization of a serine endopeptidase from rat liver plasma membranes;Biochimica et Biophysica Acta (BBA) - General Subjects;1986-04
4. Guanidinobenzoatase as a Marker for Tumour Cells;Protides of the Biological Fluids;1984
5. Characterization of tumor cell membrane serine proteases by polyacrylamide gel electrophoresis.;Journal of Histochemistry & Cytochemistry;1983-10
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