Characterization of weak protein dimerization by direct analysis of sedimentation equilibrium distributions: The INVEQ approach

2007 ◽  
Vol 368 (2) ◽  
pp. 168-177 ◽  
Author(s):  
Donald J. Winzor ◽  
Peter R. Wills
2000 ◽  
Vol 51 (2) ◽  
pp. 183 ◽  
Author(s):  
Maria Byrne ◽  
Peter A. Vesk

The Australian freshwater mussel Hyridella depressa sequesters elements in calcium phosphate (CaP) granules that form extensive aggregations in its tissues. Elements contained in these granules were determined by X-ray microanalysis of river and lake mussels from the Hawkesbury–Nepean River system, New South Wales. Granules in freeze-substituted mantle tissue were analysed to determine the variation in element profiles in granules among mussels and among sites. For the common elements Ca, P, Fe, Mg and Mn, granule composition reflected catchment lithology and site trophic status and indicated exogenous input. These were most important for differentiation among lake sites and also indicated differences between lake and river mussels. Site differences seen with some common elements in granules from lake mussels correlated with differences in water chemistry. Trace elements, particularly Al, Cu, Zn and Pb, were also important in lake and river site differentiation. The granules play a major role in element dynamics in freshwater mussel tissues and provide a focal structure for direct analysis of element accumulation by these bivalves. The results indicate that characterization of element content of granules in mussel populations would provide valuable insights into animal–element interactions in freshwater systems for ecological and ecotoxicological investigations.


2021 ◽  
Author(s):  
Sneha Gopalan ◽  
Yuqing Wang ◽  
Nicholas W. Harper ◽  
Manuel Garber ◽  
Thomas G Fazzio

Methods derived from CUT&RUN and CUT&Tag enable genome-wide mapping of the localization of proteins on chromatin from as few as one cell. These and other mapping approaches focus on one protein at a time, preventing direct measurements of co-localization of different chromatin proteins in the same cells and requiring prioritization of targets where samples are limiting. Here we describe multi-CUT&Tag, an adaptation of CUT&Tag that overcomes these hurdles by using antibody-specific barcodes to simultaneously map multiple proteins in the same cells. Highly specific multi-CUT&Tag maps of histone marks and RNA Polymerase II uncovered sites of co-localization in the same cells, active and repressed genes, and candidate cis-regulatory elements. Single-cell multi-CUT&Tag profiling facilitated identification of distinct cell types from a mixed population and characterization of cell type-specific chromatin architecture. In sum, multi-CUT&Tag increases the information content per cell of epigenomic maps, facilitating direct analysis of the interplay of different proteins on chromatin.


2017 ◽  
Vol 9 (34) ◽  
pp. 5044-5051 ◽  
Author(s):  
Ifeoluwa Ayodeji ◽  
Timothy Vazquez ◽  
Ronelle Bailey ◽  
Theresa Evans-Nguyen

Herein, DART ionization was coupled to DMS to demonstrate their combined utility and compatibility for rapid separation and characterization of new psychoactive substances.


1988 ◽  
Vol 250 (2) ◽  
pp. 453-458 ◽  
Author(s):  
H Sobek ◽  
H Görisch

A heat-stable esterase has been purified 1080-fold to electrophoretic homogeneity from Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium; 20% of the starting activity is recovered. The purified enzyme shows a specific activity of 158 units/mg, based on the hydrolysis of p-nitrophenyl acetate. The esterase hydrolyses short-chain p-nitrophenyl esters, aliphatic esters and triacylglycerols. It is strongly inhibited by paraoxon and phenylmethanesulphonyl fluoride, but only weakly by eserine. From sedimentation-equilibrium data and molecular sieving in polyacrylamide gels, the Mr of the esterase is estimated to be 117000-128000. SDS/polyacrylamide-gel electrophoresis reveals a single band of protein, of Mr 32000. The purified esterase crystallizes in the presence of poly(ethylene glycol) in short rods. The enzyme is inactivated only on prolonged storage at temperature above 90 degrees C.


2019 ◽  
Vol 68 (7) ◽  
pp. 483-490
Author(s):  
Chikako TAKEI ◽  
Kenichi YOSHIZAWA ◽  
Sayaka NAKAMURA ◽  
Thierry FOUQUET ◽  
Hiroaki SATO

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