Measurement and DFT Calculation of Fe(cp)2Redox Potential in Molecular Monolayers Covalently Bound to H−Si(100)

2006 ◽  
Vol 110 (46) ◽  
pp. 22961-22965 ◽  
Author(s):  
M. Cossi ◽  
M. F. Iozzi ◽  
A. G. Marrani ◽  
T. Lavecchia ◽  
P. Galloni ◽  
...  
Keyword(s):  
Dft Calculation ◽  
Molecular Monolayers ◽  
Covalently Bound

Tuning the redox potential in molecular monolayers covalently bound to H–Si(100) electrodes via distinct C–C tethering arms

2008 ◽  
Vol 44 (4-5) ◽  
pp. 542-549 ◽  
Author(s):  
R. Zanoni ◽  
M. Cossi ◽  
M.F. Iozzi ◽  
F. Cattaruzza ◽  
E.A. Dalchiele ◽  
...  
Keyword(s):  
Redox Potential ◽  
Molecular Monolayers ◽  
Covalently Bound

Adsorption of Fibrinogen and Fragment D of Fibrinogen onto the Insolubilized αChain of Fibrin

1979 ◽  
Vol 41 (04) ◽  
pp. 687-690
Author(s):  
F R Matthias
Keyword(s):  
Disulfide Bridges ◽  
Soluble Fibrin ◽  
Immobilized Proteins ◽  
Covalently Bound

SummaryAfter thrombin treatment insolubilized fibrinmonomer, which is obtained from insolubilized fibrinogen covalently bound to agarose, adsorbs soluble fibrin and its derivatives from solutions. The immobilized proteins are attached to the agarose by the ‘A’ αchain. After reduction of the disulfide bridges the β and γchains can be removed from the agarose.After thrombin treatment the immobilized αchain adsorbs fibrinogen and fragment D. To some extent the β and γchain do not seem necessary for the adsorption. The amount adsorbed increases, when thrombin treatment of the insolubilized protein follows the reduction process.This may indicate that the fibrinopeptides ‘A’ of the insolubilized αchain are better accessible after the removal of the β and γchains.

INTERFERENCE BY SERUM PROTEINS WITH LH RADIOIMMUNOASSAY USING IMMUNOSORBENT

1973 ◽  
Vol 72 (2) ◽  
pp. 235-242 ◽  
Author(s):  
A. M. Reuter ◽  
J. C. Hendrick ◽  
J. Sulon ◽  
P. Franchimont
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
High Molecular Weight ◽  
Serum Proteins ◽  
Void Volume ◽  
High Molecular Weight Proteins ◽  
Serum Fractionation ◽  
Covalently Bound

ABSTRACT The percentage of LH* bound to antibodies that have been covalently bound to cellulose is diminished in the presence of LH-free human serum and sera from various species of animals. Serum fractionation studies on Sephadex G 200 show that the greatest interference comes from the proteins eluted in the void volume i. e. the high molecular weight proteins. Specifically, the gamma M globulins and the α2-macroglobulins appear to play an important role, as demonstrated by tests in which these proteins were neutralized by gamma M and α2-macroglobulin antisera.

COMPARISON BETWEEN COVALENTLY BOUND AND FREE ANTIBODIES, USED FOR RADIOIMMUNOASSAY

1971 ◽  
Vol 68 (3) ◽  
pp. 425-430 ◽  
Author(s):  
J. Arends
Keyword(s):  
Covalently Bound

ABSTRACT Radioimmunoassays using either free or covalently bound antibodies under otherwise identical conditions have been compared. A lowered utilization of antibodies and a loss in sensitivity protential have been observed with the last mentioned method.

scholarly journals Mechanochemical Release of Non‐Covalently Bound Guests from a Polymer‐Decorated Supramolecular Cage

2021 ◽  
Author(s):  
Robin Küng ◽  
Tobias Pausch ◽  
Dustin Rasch ◽  
Robert Göstl ◽  
Bernd M. Schmidt
Keyword(s):  
Covalently Bound
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