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Lysis

About: Lysis is a research topic. Over the lifetime, 6072 publications have been published within this topic receiving 216978 citations.


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Journal ArticleDOI
TL;DR: Chlorine showed the strongest ability to impair the cell integrity with a majority (≥ 88%) of the cells compromised within the first minute and with the cell lysis rates ranging of 0.640-3.82 h(-1) during 1-60 min.

178 citations

Journal ArticleDOI
TL;DR: The extrapolated zero time intercepts of these reactions suggested that two-thirds of cellular glyceraldehyde-3-P dehydrogenase was membrane bound prior to hemolysis, similar to that calculated for the association of the enzyme with band 3 in the intact red cell when the high ionic strength and enzyme-eluting compounds in the cytoplasm are taken into account.

177 citations

Journal ArticleDOI
TL;DR: It is suggested that in vivo the cell adhesion factor is stored in the secretory granules of the semigranular and the granular cells in a putative inactive pro-form, which can be released during exocytosis and activated outside the cells to mediate cell attachment and spreading, processes of essential importance in arthropod host defense.
Abstract: Isolated granular haemocytes (blood cells) from the crayfish Pacifastacus leniusculus attached and spread in vitro on coverslips coated with a lysate of crayfish haemocytes. No cell adhesion activity was detected in crayfish plasma. The cell adhesion activity was only present in haemocyte lysates in which the prophenoloxidase (proPO) activating system (Soderhall and Smith, 1986a, b) had been activated; either by lipopolysaccharide (LPS), the beta-1,3-glucan laminarin, or by preparing the lysate in 5 mM Ca2+. Both lysates of granular or of semigranular haemocytes could mediate adhesion. After A23187-induced exocytosis of the granular cells, cell adhesion activity could be generated in the secreted material if it was incubated with laminarin. The factor responsible for cell adhesion was isolated from an active haemocyte lysate and purified by ammonium sulfate precipitation, cation exchange chromatography and Con A-Sepharose; it had a molecular mass of approximately 76 kD on an SDS-polyacrylamide gel. An antibody to this 76-kD band inhibited cell adhesion. Ca2+ was necessary in the medium for the cells to adhere to the adhesion factor. With cyanide or azide, the cells attached but failed to spread. It is suggested that in vivo the cell adhesion factor is stored in the secretory granules of the semigranular and the granular cells in a putative inactive pro-form, which can be released during exocytosis and, in the presence of beta-1,3-glucans or LPS, be activated outside the cells to mediate cell attachment and spreading, processes of essential importance in arthropod host defense.

177 citations

Journal ArticleDOI
TL;DR: Two independent mutants of Escherichia coli lacking murein-lipoprotein have been found in this paper, one of which was named lpo and the other was known as lpo.
Abstract: Two independent mutants of Escherichia coli lacking murein-lipoprotein have been found One mutant whose mutation was named lpo was subjected to detailed analyses The absence of both found and unbound lipoproteins was shown by electrophoretic analysis of 14C-arginine labelled membrane proteins of the mutant Nor was serologically cross-reacting material detected in the mutant by the Ouchterlony-method Sequestering magnesium from mutant cell suspensions by ethylenediaminetetraacetic acid caused cell lysis, which was prevented in the presence of 05 M sucrose Incubation in culture media at a very low level of magnesium resulted in the formation of blebs in the mutant Examination of mutant cells by electron microscopy showed that the outer membrane of the mutant was uneven with small irregular protuberances, some of which pinched off forming vesicles of various sizes Phosphotungstate used for negative-staining penetrated into the periplasmic space of the mutant cells The mutants leaked a considerable fraction of their periplasmic enzymes These physiological and morphological alterations in the lipoproteinless mutant suggest that murein-lipoprotein helps to maintain the outer envelope structure by connecting the outer membrane with murein so that the outer membrane may fulfil its physiological functions as a barrier to the environment

177 citations

Journal ArticleDOI
TL;DR: Data indicate that high-affinity membrane binding-sites with specificity for E2β must be further considered in investigations of the uterine cell recognition of and response to the hormone.

176 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023389
2022607
2021123
2020142
2019139
2018161