Intracellular, high-affinity binding proteins for chlorinated dioxins and related compounds — A concluding remark

Chemosphere ◽  
1987 ◽  
Vol 16 (8-9) ◽  
pp. 2187-2190 ◽  
Author(s):  
Lorenz Poellinger
Keyword(s):  
Binding Proteins ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity ◽  
Chlorinated Dioxins ◽  
Related Compounds

Shark Attack: High affinity binding proteins derived from shark vNAR domains by stepwise in vitro affinity maturation

2014 ◽  
Vol 191 ◽  
pp. 236-245 ◽  
Author(s):  
Stefan Zielonka ◽  
Niklas Weber ◽  
Stefan Becker ◽  
Achim Doerner ◽  
Andreas Christmann ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Affinity Maturation ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

Selecting high-affinity binding proteins by monovalent phage display

Biochemistry ◽  
1991 ◽  
Vol 30 (45) ◽  
pp. 10832-10838 ◽  
Author(s):  
Henry B. Lowman ◽  
Steven H. Bass ◽  
Nancy Simpson ◽  
James A. Wells
Keyword(s):  
Phage Display ◽  
Binding Proteins ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

scholarly journals Novel Ubiquitin-derived High Affinity Binding Proteins with Tumor Targeting Properties

2014 ◽  
Vol 289 (12) ◽  
pp. 8493-8507 ◽  
Author(s):  
Susan Lorey ◽  
Erik Fiedler ◽  
Anja Kunert ◽  
Jörg Nerkamp ◽  
Christian Lange ◽  
...  
Keyword(s):  
Tumor Targeting ◽  
Binding Proteins ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

scholarly journals Binding proteins for adenosine 3′:5′-cyclic monophosphate in bovine adrenal cortex

1977 ◽  
Vol 165 (3) ◽  
pp. 561-573 ◽  
Author(s):  
Stein Ove Døskeland ◽  
Per Magne Ueland
Keyword(s):  
Ionic Strength ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Adrenal Cortex ◽  
Binding Proteins ◽  
Catalytic Subunit ◽  
Regulatory Subunit ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

Five peaks of cyclic AMP-binding activity could be resolved by DEAE-cellulose chromatography of bovine adrenal-cortex cytosol. Two of the binding peaks co-chromatographed with the catalytic activities of cyclic AMP-dependent protein kinases (ATP–protein phosphotransferase, EC 2.7.1.37) of type I or type II respectively. A third binding protein was eluted between the two kinases, and appeared to be the free regulatory moiety of protein kinase I. Two of the binding proteins for cyclic AMP, sedimenting at 9S in sucrose gradients, could also bind adenosine. They bound cyclic AMP with an apparent equilibrium dissociation constant (Kd) of about 0.1μm, and showed an increased binding capacity for cyclic AMP after preincubation in the presence of K+, Mg2+ and ATP. The two binding proteins differed in their apparent affinities for adenosine. The isolated regulatory moiety of protein kinase I had a very high affinity for cyclic AMP (Kd<0.1nm). At low ionic strength or in the presence of MgATP, the high-affinity binding of cyclic AMP to the regulatory subunit of protein kinase I was decreased by the catalytic subunit. At high ionic strength and in the absence of MgATP the high-affinity binding to the regulatory subunit was not affected by the presence of catalytic subunit. Under all experimental conditions tested, dissociation of protein kinase I was accompanied by an increased affinity for cyclic AMP. To gain some insight into the mechanism by which cyclic AMP activates protein kinase, the interaction between basic proteins, salt and the cyclic nucleotide in activating the kinase was studied.

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