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Isoelectric focusing by free solution capillary electrophoresis.
- Source :
-
Analytical biochemistry [Anal Biochem] 1992 Oct; Vol. 206 (1), pp. 84-90. - Publication Year :
- 1992
-
Abstract
- A reproducible, quantitative isoelectric focusing method using capillary electrophoresis that exhibits high resolution and linearity over a wide pH gradient was developed. RNase T1 and RNase ba are two proteins that have isoelectric points (pI's) at the two extremes of a pH 3-10 gradient. Site-directed mutants of the former were separated from the wild-type form and pI's determined in the same experiment. The pI's of RNase T1 wild-type, its three mutants, and RNase ba were determined for the first time as 2.9, 3.1, 3.1, 3.3, and 9.0, respectively. The paper describes the protocol for isoelectric focusing by capillary electrophoresis, as well as presenting data describing the linearity, resolution, limits of mass loading, and reproducibility of the method.
- Subjects :
- Bacterial Proteins
Carbonic Anhydrases isolation & purification
Cholecystokinin isolation & purification
Drug Stability
Electrophoresis
Hydrogen-Ion Concentration
Isoelectric Focusing methods
Lactoglobulins isolation & purification
Peptide Fragments isolation & purification
Reproducibility of Results
Ribonuclease T1 isolation & purification
Ribonuclease, Pancreatic isolation & purification
Ribonucleases isolation & purification
Proteins isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 0003-2697
- Volume :
- 206
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Analytical biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 1456446
- Full Text :
- https://doi.org/10.1016/s0003-2697(05)80014-4