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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Blackwell Publishing Ltd
1990
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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. |
format | Online Article Text |
id | pubmed-5918091 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | Blackwell Publishing Ltd |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT chungsungmin variantcathepsinlactivityfromgastriccancertissue |