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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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Detalles Bibliográficos
Autor principal: Weiss, Leonard
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1966
Materias:
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.
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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
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