Results 161 to 170 of about 149,683 (183)

Interactions of Alcohol Dehydrogenase to p‐Hydroxyacetophenone–sepharose and p‐Acetamidophenol‐sepharose

Alcoholism: Clinical and Experimental Research, 2005
Abstract: Background: p‐Hydroxyacetophenone (HAP)‐sepharose is known to be an effective ligand for isolation of aldehyde dehydrogenase and chloramphenicol acetyltransferase. In this study, we investigated ligand specificities to alcohol dehydrogenase (ADH) using p‐HAP‐sepharose and p‐acetamidophenol (AAP)‐sepharose.Methods: p‐HAP and p‐AAP were ...
Ichiro Wakabayashi, Munetaka Negoro
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Preparation of sepharose-bound poly (rI:rC)

Biochemical and Biophysical Research Communications, 1971
Abstract Poly rI was covalently bound through its terminal 5′-phosphate moiety to Sepharose and then annealed with poly rC to yield insoluble matrix bound poly (rI:rC). The method has no serious deleterious effects on the integrity or in vitro biological activity of the double stranded complexes.
Robert L. Bugianesi, Arthur F. Wagner, T.Y. Shen   +2 more
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Chromatography of vWF on dextran sulphate sepharose

Thrombosis Research, 1987
A relatively simple and reproducible chromatographic separation using Dextran Sulphate (DS) Agarose is described for the purification of vWf:Ag from cryoprecipitate or plasma source material. The elution profiles suggest high affinity of vWf for the matrix permitting resolution from Fibrinogen, IgG and the unbound Albumin.
Paul Harrison, G. F. Savidge, R.H. Saundry   +2 more
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Continuous spectrophotometric assay of a Sepharose-bound enzyme and its use to study kinetics of coupling of the enzyme to sepharose

Analytical Biochemistry, 1973
Abstract Continuous spectrophotometric assay of Sepharose-bound aldolase was performed using a commercial spectrophotometer with a built-in magnetic stirrer. Under most conditions likely to be encountered, the turbidity of the stirred Sepharose suspension did not interfere significantly with the optical measurements.
D.K.K. Chong, William W.-C. Chan, John S. Mort   +2 more
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Purification of Immunoglobulins Using Protein A-Sepharose

2003
Most immunochemical techniques used in molecular biology rely on a specific class of antibodies, immunoglobulin G (IgG). In mammals, IgG antibodies are produced during the secondary humoral response and contribute about 80% of the serum immunoglobulin. Factors affecting the experimental production of antibodies have been discussed in detail (1).
John B. W. Hammond, Nicholas J. Kruger
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Inactivation of aminated horseradish peroxidase by interaction with S-Sepharose

Analytical Biochemistry, 1991
Horseradish peroxidase which had been aminated by periodate oxidation and reductive amination was purified by cation-exchange chromatography on S-Sepharose. Instead of the expected single peak of aminated enzyme, two distinct peaks of protein were eluted from the column. Evaluation of the protein in each of the two distributions showed that peak number
Sae H. Choo, Michael P. Allen, Richard F. Parrish, Thomas M. Li   +3 more
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Tamisage moléculaire sur Sepharose 6B

Journal of Chromatography A, 1974
Abstract Molecular filtration on Sepharose 6B. Empiric relationships between the distribution coefficient and the Stokes radius on the one hand and the molecular weight on the other of proteins of different degrees of asymmetry The distribution coefficient, K d , of macromolecular proteins as determined by Sepharose 6B filtration is a linear ...
Sylvain Demassieux, Jean-Paul Lachance
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Interferon-sepharose: Induction of the antiviral state

Biochemical and Biophysical Research Communications, 1974
Summary Mouse (L cell) interferon has been covalently attached to Sepharose beads. The interferon-Sepharose beads induce resistance in L cells to virus replication. It is concluded that interferon induces resistance to viral replication from the cell surface only without entry into the cell.
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Ion-exchange properties of cibacron blue 3G-A sepharose (blue sepharose) and the interaction of proteins with cibacron blue 3g-a

Journal of Chromatography A, 1984
The affinity for Blue Sepharose of several proteins of known structure showed a pH dependence governed by their isoelectric points; Blue Sepharose behaved like a strong cationic ion exchanger because of the negative charges of its dye ligand, Cibacron Blue.
Ileana Abrudan, Marius Telia, Horea Porumb, Ioan Lascu, Ioan Petrescu, Cornelia Tarmure, Tudor Porumb, Ioan Proinov, Elena Presecan   +8 more
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PHOTOSENSITIZING EFFECTS OF HEMATOPORPHYRIN DERIVATIVE IMMOBILIZED ON SEPHAROSE

Photochemistry and Photobiology, 1987
Abstract— The cytotoxicity that ensues following photosensitization by hematoporphyrin derivative (Hpd) is attributed to production of singlet oxygen. Many of the cellular end points reported to be affected are localized to membranes, hydrophobic environments conducive to partitioning of hydrophobic porphyrins in Hpd.
Russell Hilf, Scott L. Gibson, Richard S. Murant   +2 more
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