scholarly journals Identification of HMGB1-Binding Components Using Affinity Column Chromatography

10.5772/56336 ◽  
2013 ◽  
Author(s):  
Ari Rouhiainen ◽  
Helena Tukiainen ◽  
Pia Siljander ◽  
Heikki Rauval
Keyword(s):  
Column Chromatography ◽  
Affinity Column ◽  
Affinity Column Chromatography

scholarly journals Purification of human erythrocyte adenosine deaminase by affinity column chromatography.

1976 ◽  
Vol 251 (13) ◽  
pp. 4026-4032 ◽  
Author(s):  
W P Schrader ◽  
A R Stacy ◽  
B Pollara
Keyword(s):  
Adenosine Deaminase ◽  
Column Chromatography ◽  
Human Erythrocyte ◽  
Affinity Column ◽  
Affinity Column Chromatography

Specific binding of immunoglobulin G to protein A–mesoporous silica composites for affinity column chromatography

2013 ◽  
Vol 1 (45) ◽  
pp. 6321 ◽  
Author(s):  
Kazuma Nakanishi ◽  
Masahiro Tomita ◽  
Hitomi Nakamura ◽  
Katsuya Kato
Keyword(s):  
Mesoporous Silica ◽  
Column Chromatography ◽  
Immunoglobulin G ◽  
Specific Binding ◽  
Protein A ◽  
Affinity Column ◽  
Affinity Column Chromatography

scholarly journals Aldolase potentiates DIDS activation of the ryanodine receptor in rabbit skeletal sarcoplasmic reticulum

2006 ◽  
Vol 399 (2) ◽  
pp. 325-333 ◽  
Author(s):  
In-Ra Seo ◽  
Sang Hyun Moh ◽  
Eun Hui Lee ◽  
Gerhard Meissner ◽  
Do Han Kim
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Column Chromatography ◽  
Anion Channel ◽  
Affinity Column ◽  
Open Probability ◽  
Release Channel ◽  
Affinity Column Chromatography ◽  
Lifetime Analysis ◽  
Associated Proteins

DIDS (4,4′-di-isothiocyanostilbene-2,2′-disulfonate), an anion channel blocker, triggers Ca2+ release from skeletal muscle SR (sarcoplasmic reticulum). The present study characterized the effects of DIDS on rabbit skeletal single Ca2+-release channel/RyR1 (ryanodine receptor type 1) incorporated into a planar lipid bilayer. When junctional SR vesicles were used for channel incorporation (native RyR1), DIDS increased the mean Po (open probability) of RyR1 without affecting unitary conductance when Cs+ was used as the charge carrier. Lifetime analysis of single RyR1 activities showed that 10 μM DIDS induced reversible long-lived open events (Po=0.451±0.038) in the presence of 10 μM Ca2+, due mainly to a new third component for both open and closed time constants. However, when purified RyR1 was examined in the same condition, 10 μM DIDS became considerably less potent (Po=0.206±0.025), although the caffeine response was similar between native and purified RyR1. Hence we postulated that a DIDS-binding protein, essential for the DIDS sensitivity of RyR1, was lost during RyR1 purification. DIDS-affinity column chromatography of solubilized junctional SR, and MALDI–TOF (matrix-assisted laser-desorption ionization–time-of-flight) MS analysis of the affinity-column-associated proteins, identified four major DIDS-binding proteins in the SR fraction. Among them, aldolase was the only protein that greatly potentiated DIDS sensitivity. The association between RyR1 and aldolase was further confirmed by co-immunoprecipitation and aldolase-affinity batch-column chromatography. Taken together, we conclude that aldolase is physically associated with RyR1 and could confer a considerable potentiation of the DIDS effect on RyR1.

Fractionation of Glycopeptides by Affinity Column Chromatography on Concanavalin A-Sepharose1

1975 ◽  
Vol 78 (4) ◽  
pp. 687-696 ◽  
Author(s):  
Shun-ichiroh OGATA ◽  
Takashi MURAMATSU ◽  
Akira KOBATA
Keyword(s):  
Column Chromatography ◽  
Concanavalin A ◽  
Affinity Column ◽  
Affinity Column Chromatography
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