A protein network for phospholipid synthesis uncovered by a variant of the tandem affinity purification method inEscherichia coli

PROTEOMICS ◽  
2006 ◽  
Vol 6 (1) ◽  
pp. 282-293 ◽  
Author(s):  
Djamel Gully ◽  
Emmanuelle Bouveret
Keyword(s):  
Affinity Purification ◽  
Tandem Affinity Purification ◽  
Protein Network ◽  
Inescherichia Coli ◽  
Phospholipid Synthesis ◽  
Purification Method

scholarly journals Identification of Proteins Interacting with Dysferlin Using the Tandem Affinity Purification Method

2008 ◽  
Vol 1 ◽  
pp. 17-23 ◽  
Author(s):  
Maziar Assadi ◽  
Thomas Schindler ◽  
Bernd Muller ◽  
John D Porter ◽  
Markus A Ruegg ◽  
...  
Keyword(s):  
Affinity Purification ◽  
Tandem Affinity Purification ◽  
Purification Method

Isolation of Human Fibrinogen and its Derivatives by Affinity Chromatography on Gly-Pro-Arg-Pro-Lys-Fractogel

1990 ◽  
Vol 63 (03) ◽  
pp. 439-444 ◽  
Author(s):  
C Kuyas ◽  
A Haeberli ◽  
P Walder ◽  
P W Straub
Keyword(s):  
Gel Electrophoresis ◽  
Affinity Purification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ease Of Use ◽  
Terminal Sequence ◽  
Purification Method ◽  
Human Fibrinogen ◽  
Isolation Methods ◽  
One Step ◽  
Complementary Binding

SummaryWith an immobilized synthetic pentapeptide GlyProArgProLys comprising the N-terminal sequence GlyProArg of the α-chain of fibrin, a new affinity method for the quantitative isolation of fibrinogen out of anticoagulated plasma was developed. The method proved to be superior to all known isolation methods in respect to ease of use and yield, since fibrinogen could be isolated in one step out of plasma with a recovery of more than 95% when compared to the immunologically measurable amounts of fibrinogen. Moreover the amounts of contaminating proteins such as fibronectin, factor XIII or plasminogen were negligible and the purity of the isolated fibrinogen was higher than 95% as measured by polyacrylamide gel electrophoresis. The clottability was 90% and more. Another advantage of this affinity purification method is the possibility to isolate fibrinogen quantitatively out of small plasma samples (<5 ml). Further, abnormal fibrinogen molecules, provided their complementary binding site for GlyProArg is preserved, may also be quantitatively isolated independent of any solubility differences as compared to normal fibrinogen. In addition fibrin(ogcn) fragments originating from plasmic digestion can be separated on the basis of their affinity to GlyProArg. The described affinity gel can be used more than 50 times without any loss of capacity.

scholarly journals Tandem affinity purification in Drosophila: the advantages of the GS-TAP system

Fly ◽  
2008 ◽  
Vol 2 (4) ◽  
pp. 229-235 ◽  
Author(s):  
Phillip P. Kyriakakis ◽  
Marla Tipping ◽  
Louka Abed ◽  
Alexey Veraksa
Keyword(s):  
Affinity Purification ◽  
Tandem Affinity Purification

Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo

PROTOPLASMA ◽  
2016 ◽  
Vol 254 (4) ◽  
pp. 1547-1562 ◽  
Author(s):  
Jana Majerská ◽  
Petra Procházková Schrumpfová ◽  
Ladislav Dokládal ◽  
Šárka Schořová ◽  
Karel Stejskal ◽  
...  
Keyword(s):  
Affinity Purification ◽  
Tandem Affinity Purification ◽  
Interaction Partners
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