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Comparative Study
. 1990 Aug;81(8):813-9.
doi: 10.1111/j.1349-7006.1990.tb02650.x.

Variant cathepsin L activity from gastric cancer tissue

S M Chung  1
Affiliations
Comparative Study

Variant cathepsin L activity from gastric cancer tissue

S M Chung. Jpn J Cancer Res. 1990 Aug.

Abstract

Cathepsin L activity was partially purified by S-Sepharose FF chromatography, concanavalin-A Sepharose chromatography, phenyl-Superose column chromatography, Mono S column chromatography, and TSK G3000SWXL column chromatography from gastric cancer tissue. The optimal pH of cathepsin L from gastric cancer tissue was 7.4, and the activity was retained even at alkaline pH. Heat stability tests showed that cathepsin L from gastric cancer tissue was heat stable; that is, 65% activity was retained after incubation at 56 degrees C for 60 min. The molecular weight of cathepsin L from gastric cancer tissue was estimated as 115 kD by gel filtration or 110 kD by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme showed a different affinity for wheat germ agglutinin-Sepharose than cathepsin L from gastric normal mucosa. These results suggest that cathepsin L from gastric cancer tissue may play an important role in gastric cancer invasion through the destruction of the surrounding extracellular matrix by its proteolytic activity.

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