PMID: 7560Aug 10, 1976

Purification and properties of cathepsin D from porcine spleen.

The Journal of Biological Chemistry
M Cunningham, J Tang

Abstract

Cathepsin D was purified from porcine spleen to near homogeneity as determined by gel electrophoresis. The isolation scheme involved an acid precipitation of tissue extract, DEAE-cellulose and Sephadex G-200 chromatography, and isoelectric focusing. The end product represented about a 1000-fold purification and about a 10% recovery. The purified enzyme was the major isoenzyme, which represented 60% of cathepsin D present in porcine spleen. Two minor isoenzymes of cathepsin D were present in small amounts. The purified enzyme resembled porcine pepsin in molecular weight (35,000), amino acid composition, and inactivation by specific pepsin inactivators. The pH activity curve of the purified enzyme showed two optima near pH 3 and 4. The relative activities at these optimal pH values were affected by salt concentration. Experimental evidence indicated that the two-optima phenomenon is a property of a single enzyme species.

Related Concepts

Amino Acid Sequence
Amino Acids
Metazoa
Cathepsins
Fluram
Hydrogen-Ion Concentration
Alloenzymes
Kinetics
Molecular Weight
Peptide Fragments

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