Isolation and partial characterization of cathepsin C extracted from bovine spleen and muscle tissue

Abstract

Cathepsin C was extracted from fetal bovine muscle and adult bovine spleen and muscle by a modification of the acid extraction method of De La Haba et al. (1955). Further purification of the cathepsin C extract was accomplished by gel filtration through utilization of Sephadex G-100 separation followed by a Sephadex G-200 separation. A 0.05 M sodium citrate buffer at pH 4.85 in 0.9 percent NaCl was utilized in both steps of gel filtration. Final purification of the enzyme was accomplished by electrophoresis at pH 4.5 in a preparative E-C Vertical Electrophoresis Cell. The pH stability of the enzyme is maximum in a range of pH 3.5-7.0. Activity decreases sharply to zero at 1.5 pH units on either side of this pH range. ...