6-Aminohexyl–Agarose
6-Aminohexyl–Agarose structure
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Common Name | 6-Aminohexyl–Agarose | ||
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| CAS Number | 58856-73-8 | Molecular Weight | N/A | |
| Density | 1.026 g/mL at 20 °C | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Protection against Trp-P-2 mutagenicity by purpurin: mechanism of in vitro antimutagenesis.
Mutagenesis 15(3) , 223-228, (2000) Purpurin (1,2,4-trihydroxy-9,10-anthraquinone) is a natural pigment isolated from madder root (Rubia tinctorum) which inhibits the mutagenicity of a number of heterocyclic amines in the Ames mutagenicity test. Two effects were observed in the presence of purp... |
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Purification to apparent homogeneity and properties of pig kidney L-fucose kinase.
J. Biol. Chem. 273(10) , 5685-5691, (1998) L-Fucokinase was purified to apparent homogeneity from pig kidney cytosol. The molecular mass of the enzyme on a gel filtration column was 440 kDa, whereas on SDS gels a single protein band of 110 kDa was observed. This 110-kDa protein was labeled in a concen... |
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Lactoferrin: similarity to diamine oxidase and purification by aminohexyl affinity chromatography.
Eur. J. Biochem. 241(1) , 303-8, (1996) A protein reacting with a monoclonal antibody against human placental diamine oxidase was purified from the specific granules of human neutrofil granulocytes using affinity chromatography on aminohexyl-divinylsulfonyl-agarose. The protein had an M(r) determin... |
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Serum amine oxidase can specifically recognize and oxidize aminohexyl (AH) chains on AH-Sepharose support: single-step affinity immobilization.
Biotechnol. Appl. Biochem. 28 ( Pt 2) , 99-104, (1998) Preparative affinity chromatography of bovine serum amine oxidase (SAO) on aminohexyl (AH)-Sepharose was often associated with an unexpected irreversible SAO retention on the support. This particular enzyme immobilization, occurring without coupling reagents,... |
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Isolation of amine oxidase from bovine plasma by a two-step procedure.
Protein Expr. Purif. 3(5) , 362-7, (1992) A novel method for isolation of amine oxidase from bovine plasma is reported; it involves a two-step procedure, namely ammonium sulfate fractionation and affinity chromatography with elution by aniline, which is a competitive inhibitor of the enzyme. A homoge... |
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Quantitation of adsorption capacity of immunoglobulin G on histidine-aminohexyl sepharose and determination of affinity constant.
J. Chromatogr. A. 616(2) , 189-95, (1993) Histidine, a pseudobiospecific ligand, had been utilized to purify several proteins such as chymosin, acidic protease, carboxypeptidase Y and immunoglobulin G (IgG). A detailed study was undertaken to purify IgG on histidine coupled to aminohexyl Sepharose [A... |
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Purification of human IgG by negative chromatography on omega-aminohexyl-agarose.
J. Chromatogr. B. Analyt. Technol. Biomed. Life Sci. 878(5-6) , 557-66, (2010) A novel method for spectrometrical measurement of myeloperoxidase (MPO) activity in plasma with o-dianisidine (DA) as a substrate is proposed. We have determined the optimal conditions, including the pH and hydrogen peroxide concentration, under which MPO is ... |
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Purification of recombinant HIV-1 protease.
Prep. Biochem. 21(2-3) , 163-73, (1991) A method is described to purify recombinant HIV-1 protease from soluble extracts of Escherichia coli. The isolation involves QAE-Sepharose anion exchange chromatography, hexyl agarose hydrophobic interaction chromatography, MonoS cation exchange chromatograph... |
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A rapid purification of bovine testicular hyaluronidase by chromatography on dermatan sulphate-substituted 1,6-diaminohexane--sepharose 4B.
Biochem. J. 199(2) , 419-26, (1981) The binding of bovine testicular hyaluronidase to AH-Sepharose (1,6-diaminohexane--Sepharose) gels substituted with (1) dermatan sulphate, (2) desulphated dermatan sulphate, (3) heparin and (4) de-N/O-sulphated, re-N-acetylated heparin was investigated. Hyalu... |
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New ligands for human C-reactive protein: calcium-dependent binding with epsilon-aminocaproic acid-agarose and calcium-independent binding with omega-aminohexyl-agarose.
Int. J. Tissue React. 12(2) , 71-6, (1990) Human C-reactive protein (CRP) is an acute phase protein which increases in concentration in response to inflammation. CRP has been known to bind with phosphorylcholine in a calcium-dependent manner. In this study, CRP is found to bind to affinity chromatogra... |