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- Jeppsson, Jan olof, et al.
(författare)
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Isolation and characterization of two minor fractions of α1,-antitrypsin by high-performance liquid chromatographic chromatofocusing
- 1985
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Ingår i: Journal of Chromatography A. - 0021-9673. ; 327, s. 173-177
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Tidskriftsartikel (refereegranskat)abstract
- α1-Antitrypsin is a glycoprotein that separates into five electrophoretic fractions, viz. M2, M4, M6, M7 and M8. Con A-Sepharose separates the protein into three fractions according to the branching degree of the three oligosaccharide chains. The Con A affinity is identical for M4 and M7 and for M6 and M8. Within each pair the proteins were isolated by rapid chromatofocusing. The M7 and M8 have the same carbohydrate structure as the major M4 and M6 respectively, but have lost the first five N-terminal amino acids (Glu-Asp-Pro-Glu-Gly) as compared to the majority of the protein.
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| 2. |
- Kagedal, Bertil, et al.
(författare)
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Automated high-performance liquid chromatographic determination of 5-S-cysteinyl-3,4-dihydroxyphenylalanine in urine
- 1989
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Ingår i: Journal of Chromatography A. - 0021-9673. ; 473, s. 359-370
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Tidskriftsartikel (refereegranskat)abstract
- An automated high-performance liquid chromatographic (HPLC) method has been developed for measurement of 5-S-cysteinyl-DOPA in urine (DOPA = 3,4-dihydroxyphenylalanine). The urinary sample was injected into an HPLC boronate column. With a mobile phase of 0.1 M phosphate buffer containing 0.2 mM disodium ethylenediaminetetraacetate (Na2EDTA) (pH 6.0) mixed with methanol (9:1), 5-S-cysteinyl-DOPA was adsorbed while most other compounds were washed away. By column switching, the column flow was reversed and 5-S-cysteinyl-DOPA was desorbed by a mobile phase of 0.1 M formic acid and 0.2 mM Na2EDTA at pH 3.0 and chromatographed on a reversed-phase column. The precision, as estimated from repeated analysis of an urinary sample and from duplicate analysis of a number of samples, ranged from 1.4 to 5.2% (coefficient of variation), and the analytical recovery was 93 +/- 4.1%. The method is suitable for use in the clinical laboratory.
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| 6. |
- Ohlson, Sten, et al.
(författare)
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High-Performance Liquid Affinity Chromatographic Separation of Mouse Monoclonal Antibodies with Protein A Silica
- 1987
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Ingår i: Journal of Chromatography A. - 0021-9673 .- 1873-3778. ; 397, s. 207-212
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Tidskriftsartikel (refereegranskat)abstract
- Protein A, a bacterial cell wall protein found in Staphylococcus aureus, has been widely used for the analysis of immunoglobulins. By attaching protein A to a microparticulate silica support, a rapid and efficient chromatographic sorbent has been created for the separation of monoclonal antibodies. Examples are given of rapid separations (within 10 min) of murine monoclonal antibodies, belonging to various IgG subclasses and including IgGl. The monoclonal antibodies were isolated with a high purity and with 60–90% recovery of activity. The high-performance liquid affinity chromatography technique based on protein A provides a useful method for monitoring monoclonal antibodies in crude samples, such as ascites and cell culture supernatants.
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