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STUDIES ON CELL DEFORMABILITY : II. Effects of Some Proteolytic Enzymes
Murine sarcoma 37 ascites cells were treated with the proteolytic enzymes, trypsin and chymotrypsin, after which cellular deformability and electrophoretic mobility were measured. It was shown that incubation with trypsin increased the ease with which the cells could be deformed without changing ele...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1966
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2106986/ https://www.ncbi.nlm.nih.gov/pubmed/5966177 |
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author | Weiss, Leonard |
author_facet | Weiss, Leonard |
author_sort | Weiss, Leonard |
collection | PubMed |
description | Murine sarcoma 37 ascites cells were treated with the proteolytic enzymes, trypsin and chymotrypsin, after which cellular deformability and electrophoretic mobility were measured. It was shown that incubation with trypsin increased the ease with which the cells could be deformed without changing electrophoretic mobility, and that diisopropylfluorophosphate (DFP)-trypsin was inactive, a fact which suggests that trypsin-sensitive peptide linkages help to maintain the "tension" at the cell periphery. On the other hand, chymotrypsin reduced cellular electrophoretic mobility without appreciably altering deformability. This suggests that, although chymotrypsin-sensitive bonds do not contribute to "tension," they are in some way associated with charged groups at the cell periphery. |
format | Text |
id | pubmed-2106986 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1966 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21069862008-05-01 STUDIES ON CELL DEFORMABILITY : II. Effects of Some Proteolytic Enzymes Weiss, Leonard J Cell Biol Article Murine sarcoma 37 ascites cells were treated with the proteolytic enzymes, trypsin and chymotrypsin, after which cellular deformability and electrophoretic mobility were measured. It was shown that incubation with trypsin increased the ease with which the cells could be deformed without changing electrophoretic mobility, and that diisopropylfluorophosphate (DFP)-trypsin was inactive, a fact which suggests that trypsin-sensitive peptide linkages help to maintain the "tension" at the cell periphery. On the other hand, chymotrypsin reduced cellular electrophoretic mobility without appreciably altering deformability. This suggests that, although chymotrypsin-sensitive bonds do not contribute to "tension," they are in some way associated with charged groups at the cell periphery. The Rockefeller University Press 1966-07-01 /pmc/articles/PMC2106986/ /pubmed/5966177 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Weiss, Leonard STUDIES ON CELL DEFORMABILITY : II. Effects of Some Proteolytic Enzymes |
title | STUDIES ON CELL DEFORMABILITY : II. Effects of Some Proteolytic Enzymes |
title_full | STUDIES ON CELL DEFORMABILITY : II. Effects of Some Proteolytic Enzymes |
title_fullStr | STUDIES ON CELL DEFORMABILITY : II. Effects of Some Proteolytic Enzymes |
title_full_unstemmed | STUDIES ON CELL DEFORMABILITY : II. Effects of Some Proteolytic Enzymes |
title_short | STUDIES ON CELL DEFORMABILITY : II. Effects of Some Proteolytic Enzymes |
title_sort | studies on cell deformability : ii. effects of some proteolytic enzymes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2106986/ https://www.ncbi.nlm.nih.gov/pubmed/5966177 |
work_keys_str_mv | AT weissleonard studiesoncelldeformabilityiieffectsofsomeproteolyticenzymes |