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Variant Cathepsin L Activity from Gastric Cancer Tissue

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 c...

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Detalles Bibliográficos
Autor principal: Chung, Sung min
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 1990
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5918091/
https://www.ncbi.nlm.nih.gov/pubmed/2118894
http://dx.doi.org/10.1111/j.1349-7006.1990.tb02650.x
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author Chung, Sung min
author_facet Chung, Sung min
author_sort Chung, Sung min
collection PubMed
description 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°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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spelling pubmed-59180912018-05-11 Variant Cathepsin L Activity from Gastric Cancer Tissue Chung, Sung min Jpn J Cancer Res Article 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°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. Blackwell Publishing Ltd 1990-08 /pmc/articles/PMC5918091/ /pubmed/2118894 http://dx.doi.org/10.1111/j.1349-7006.1990.tb02650.x Text en
spellingShingle Article
Chung, Sung min
Variant Cathepsin L Activity from Gastric Cancer Tissue
title Variant Cathepsin L Activity from Gastric Cancer Tissue
title_full Variant Cathepsin L Activity from Gastric Cancer Tissue
title_fullStr Variant Cathepsin L Activity from Gastric Cancer Tissue
title_full_unstemmed Variant Cathepsin L Activity from Gastric Cancer Tissue
title_short Variant Cathepsin L Activity from Gastric Cancer Tissue
title_sort variant cathepsin l activity from gastric cancer tissue
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5918091/
https://www.ncbi.nlm.nih.gov/pubmed/2118894
http://dx.doi.org/10.1111/j.1349-7006.1990.tb02650.x
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