Results 151 to 160 of about 149,683 (183)
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Immobilization of pepsinogen on Sepharose

Biotechnology Letters, 1984
Porcine pepsinogen was attached to CNBr-activated-Sepharose 4B and self-activated to form Sepharose-pepsin. The maximum loading of pepsin on Sepharose was about 43 mg of pepsin per g of freeze-dried product. Sepharose-pepsin was stable on exposure to protein substrates and had a specific activity similar to that of the free enzyme.
N. F. Haard, K. M. Shamsuzzaman
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Fractionation of Soluble Proteins Using DEAE-Sepharose, SP-Sepharose, and Phenyl Sepharose Chromatographies for Proteomics

2017
In order to simplify a complex mixture of soluble proteins from tissues, a protocol to fractionate samples prior to two-dimensional (2D) gel electrophoresis has been developed. These methods involve the use of DEAE-Sepharose, SP-Sepharose, and phenyl Sepharose chromatographic columns and the fractionation of the protein mixtures based on differential ...
Jacob S. Shaw   +2 more
openaire   +3 more sources

The Purification of Soybean 11S Globulin with ConA-Sepharose 4B and Sepharose 6B

Agricultural and Biological Chemistry, 1974
(1974). The Purification of Soybean 11S Globulin with ConA-Sepharose 4B and Sepharose 6B. Agricultural and Biological Chemistry: Vol. 38, No. 5, pp. 1083-1085.
Kazuyoshi Okubo   +2 more
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Adsorption Performance of Proteins to CM Sepharose FF and DEAE Sepharose FF Adsorbents

Korean Journal of Chemical Engineering, 2003
Adsorption equilibrium and kinetics were studied for the binding of proteins to CM Sepharose FF and DEAE Sepharose FF. The influence of temperature, pH, viscosity, initial concentration and the volume of adsorbents on the adsorption characteristics was investigated in detail.
Yi-Xin Guan, Li-Hua Yu, Shan-Jing Yao
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Selective arginase purification by Sepharose immunoabsorbent

Analytical Biochemistry, 1975
Abstract This work has shown that the method of “affinity chromatography” with antiarginase-Sepharose succesfully purifies arginase from semipurified liver extract with high yields and reproducibility.
Carmen Yuste López   +2 more
openaire   +3 more sources

Polysome Isolation by Sepharose Column Chromatography

Preparative Biochemistry, 1975
Polysomes from the mouse myeloma MOPC-21 were purified by gel filtration of Sepharose 6B, 4B and 2B columns. All three columns eliminated nearly all intracellular material smaller than 40 S subunits. In addition, passage through 4B and 2B columns substantially reduced the amount of subunits and monosomes in the preparations. Purified polysomes retained
William H. Eschenfeldt   +1 more
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Protein purification using combined streptavidin (or avidin)-Sepharose and thiopropyl-Sepharose affinity chromatography

Journal of Chromatography A, 1992
The major problem usually encountered in the application of the (strept)avidin-biotin system to the purification of proteins (or other biological molecules) lies in the difficult reversion of the interaction between immobilized (strept)avidin and the adsorbed biotinylated protein.
C Lombard   +5 more
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Induction of tyrosine aminotransferase by Sepharose-insulin

Archives of Biochemistry and Biophysics, 1974
Abstract Insulin covalently bound to Sepharose causes a nearly 2-fold increase in tyrosine aminotransferase activity in monolayer cultures of hepatoma cells previously incubated with dexamethasone. The time course of the induction and its resistance to inhibition by actinomycin D is similar to that obtained with free insulin, although approximately ...
Jeffrey L. Garwin, Thomas D. Gelehrter
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Synthesis and Use of the Protein Phosphatase Affinity Matrices Microcystin-Sepharose and Microcystin-Biotin-Sepharose

2007
Microcystin-based affinity matrices have been utilized to demonstrate the association of signaling proteins with protein phosphatases and for the purification of low-abundance microcystin-sensitive protein phosphatases. Here, we describe the procedure for the synthesis and use of microcystin-Sepharose and microcystin-biotin-Sepharose.
Moorhead, Greg B.G.   +2 more
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Peptide synthesis on SepharoseTM beads

The Journal of Peptide Research, 1997
NHS‐activated Pharmacia HiTrap SepharoseTM was modified with 1,3‐diaminopropane to give an amino‐functionalized support suitable for solid‐phase peptide synthesis. The amide linker p‐[(R,S)‐α‐[1‐(9H‐fluoren‐9‐yl)‐methoxyformamido]‐2,4‐dimethoxybenzyl]phenoxyacetic acid was incorporated and the acyl carrier protein sequence 65‐74 was synthesized ...
Ronald Frank, Werner Tegge
openaire   +3 more sources

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