Sepharose is the tradename for a cross-linked and beaded form of a polysaccharide polymer, which is extracted from seaweed. When used in research techniques (such as various forms of chromatography), iodoacetyl functional groups can be added to selectively bind the cysteine side chains in the material. This method of adding iodoacetyl functional groups is often used in procedures that require the immobilization of peptides. This brand name of polysaccharide polymer is derived from the name “Separation Pharmacia Agarose.” Sepharose is commonly used in chromatographic separations of a wide variety of biomolecules.
Sepharose is a registered trademark that belongs to GE Healthcare (the company formed from the former Pharmacia, Pharmacia Biotech, Pharmacia LKB Biotechnology, Amersham Biosciences, and Amersham Pharmacia Biotech). In the late 1950’s, Pharmacia launched Sephadex, a cross-linked dextran gel used for gel filtration. For decades, the company has continued to spearhead advances in the field of chromatography through the introduction of Sepharose in 1967.
Sepharose is known for its chemical versatility, which allows for the stable attachment of ligands for the purification of a wide variety of enzymes, antibodies, peptides, and other proteins. Because of its versatility and high mechanical stability, Sepharose is an excellent base matrix for many high performance chromatographic procedures in affinity chromatography, ion exchange chromatography, and other processes of separation.
Coupled with a particular form of activation chemistry, sepharose can also be used to immobilize many types of enzymes, antibodies, and other kinds of proteins and peptides through covalent attachment to the resin. Typical types of activation chemistry processes include the reductive animation of aldehydes (in order to attach proteins to the resin in the agarose through lysine side chains) and cyanogen bromide.
This category contains scientific information on Sepharose, a cross-linked and beaded form of a polysaccharide polymer, which is extracted from seaweed, produced and distributed by GE Healthcare.
Garbers D.L., 1982: Phosphotyrosyl protein phosphatase of tcrc 2 cells. Journal Of Biological Chemistry3: 7298-7301 Homogenization of Tcrc-2 cells yielded a phosphotyrosyl-protein phosphatase with a specific activity.apprx. 10-fold higher in particulate than in soluble fractions. Over 90% of the phosphotyrosyl-protein phophatase associated with the particles was solubilized with 1.0% Nonidet P-40. Chromatography of the detergent-solubilized [...]
Lovenberg W., 1983: Phosphorylation of brain cytosol proteins effects of phospho lipids and calmodulin. Journal Of Biological Chemistry: -1953 Calmodulin was removed from brain cytosol by Deae-52 chromatography or by affinity chromatography employing fluphenazine-Sepharose. The substrates phosphorylated by endogenous protein kinase after chromatography differed depending on the method used, and both chromatographic methods altered the [...]
Steiner M., 1979: Phosphorylation and protein kinase activity of platelet tubulin. Journal Of Biological Chemistry: 66-74 Platelet tubulin isolated by 2 successive cycles of polymerization-depolymerization contained protein kinase activity. The phosphorylating activity measured by incorporation of phosphate from Atp was cAMP-independent and behaved with respect to substrate specificity, cation requirement and maximum incorporation of phosphate [...]
Soderling, T. R.; Srivastava, A. K.; Bass, M. A.; Khatra, B. S., 1979: Phosphorylation and inactivation of glycogen synthase ec 188.8.131.52 by phosphorylase kinase ec 184.108.40.206. Proceedings of the National Academy of Sciences of the United States of America 76(6): 2536-2540 Skeletal muscle glycogen a4-synthase (Ec 220.127.116.11) was purified free of all synthase kinase and [...]
Yoshida J., 1984: Phosphorus free antihypertensive lipid from dog peritoneal dialysate peritoneal dialysate depressor ii. Journal Of Pharmacobio Dynamics: 577-585 A phosphorus-free lipid with a transient antihypertensive effect was found in a dog peritoneal dialysate by a modified procedure. On silicic acid chromatography of the crude extract, a new hypotensive factor and a new hypertensive [...]
Suzuki T., 1984: Phospholipase a 2 activity of fc gamma 2b receptors of thioglycolate elicited murine peritoneal macrophages. Journal Of Leukocyte Biology: 493-504 The detergent lysate of plastic adherent cell population of thioglycollate-elicited peritoneal exudate cells from 100 individual Swiss mice was subjected to affinity chromatography on 2 different media, Sepharose coupled to heat-aggregated human [...]
White W.R., 1981: Phospho lipid is required for the processing of pre secretory proteins by detergent solubilized canine pancreatic signal peptidase. Journal Of Biological Chemistry: 2545-2550 The ability of canine pancreatic signal peptidase to remove the signal peptide portion of presecretory proteins in a translocation-independent assay requires phospholipid. Sodium deoxycholate extracts of canine pancreatic rough [...]
Lampen J.O., 1979: Phosphatidylseryl transfer rna in bacillus licheniformis 749 c. Biochimica Et Biophysica Acta: 462-470 Phosphatidylserine was found in extracts of B. licheniformis made under alkaline conditions but not under neutral or acidic ones and was derived from the tRNA fraction. In tRNA preparations kept below neutrality during purification, phosphatidylserine was the only phospholipid [...]
Bresnick E., 1979: Persistent binding of 3 methyl cholanthrene to mouse lung dna and its correlation with susceptibility to pulmonary neoplasia. Cancer Researchpart 1: 2400-2405 A/J, C3h/HeJ, Dba/2j, and C57bl/6j mice have different susceptibilities to polycyclic aromatic hydrocarbon-induced pulmonary neoplasia, whereas the livers from these animals are uniformly resistant to the carcinogenic actions of these [...]
Acharya A.S., 1986: Permissible discontinuity region of the alpha chain of hemoglobin noncovalent interaction of heme and the complementary fragments alpha 1 30 and alpha 31 141. Biochemistry: 5949-5955 Generation of a fragment-complementing system of the.alpha.-chain on limited proteolysis with Staphylococcus aureus V8 protease has been investigated. Digestion of the.alpha.-chain (0.4 mM) of hemoglobin with [...]