Alcor BioSeparations LLC

Palo Alto, CA, United States

Alcor BioSeparations LLC

Palo Alto, CA, United States
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Dolnik V.,Alcor BioSeparations LLC | Gurske W.A.,Alcor BioSeparations LLC
Electrophoresis | Year: 2011

The paper describes a method of size separation of proteins by capillary sieving electrophoresis with cationic surfactant. Proteins are separated within 12min with repeatability of migration times better than 0.2%. Some proteins achieve the separation efficiency of 200000 theoretical plates. The method can be used for determination of protein relative molecular masses. The accuracy of the determined relative molecular masses and the limitation of the method were investigated by the analysis of more than 60 proteins. The method also allows separation of protein oligomers. Proteins can be quantitated after the electrokinetic injection in the concentration range 0.07-0.43g/L. The average detection limit is about 2mg/L. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


Dolnik V.,Alcor BioSeparations LLC | Gurske W.A.,Alcor BioSeparations LLC
Electrophoresis | Year: 2011

We studied the electrophoretic behavior of basic proteins (cytochrome c and histone III) and developed a carbamylation method that normalizes their electrophoretic size separation and improves the accuracy of their relative molecular mass determined electrophoretically. In capillary zone electrophoresis with cationic hitchhiking, native cytochrome c does not sufficiently bind cationic surfactants due to electrostatic repulsion between the basic protein and cationic surfactant. Carbamylation suppresses the strong positive charge of the basic proteins and results in more accurate relative molecular masses. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


PubMed | Alcor BioSeparations LLC
Type: Journal Article | Journal: Electrophoresis | Year: 2011

We studied the electrophoretic behavior of basic proteins (cytochrome c and histone III) and developed a carbamylation method that normalizes their electrophoretic size separation and improves the accuracy of their relative molecular mass determined electrophoretically. In capillary zone electrophoresis with cationic hitchhiking, native cytochrome c does not sufficiently bind cationic surfactants due to electrostatic repulsion between the basic protein and cationic surfactant. Carbamylation suppresses the strong positive charge of the basic proteins and results in more accurate relative molecular masses.


PubMed | Alcor BioSeparations LLC
Type: Journal Article | Journal: Electrophoresis | Year: 2011

The paper describes a method of size separation of proteins by capillary sieving electrophoresis with cationic surfactant. Proteins are separated within 12 min with repeatability of migration times better than 0.2%. Some proteins achieve the separation efficiency of 200,000 theoretical plates. The method can be used for determination of protein relative molecular masses. The accuracy of the determined relative molecular masses and the limitation of the method were investigated by the analysis of more than 60 proteins. The method also allows separation of protein oligomers. Proteins can be quantitated after the electrokinetic injection in the concentration range 0.07-0.43g/L. The average detection limit is about 2mg/L.

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