Stellan Hjertén

Research Field

Hydroxylapatite

Ultraviolet

Displacement chromatography

Ultraviolet light

10.1016/0003-9861(56)90183-7

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Citations (1,452)

A Molecular Sieving Method for Preparing Erythrocyte Membranes

Preparative Biochemistry (1980)

Gunnar Fröman Fernando Acevedo Stellan Hjertén

The most widely used methods for preparing erythrocyte membranes are time-consuming, since they involve repeated steps of centrifugation and washing. We have found that membranes can be prepared in a rapid and simple way by molecular-sieve chromatography on a Sepharose 4B column. Two sizes of columns have been used, one 9-ml column to prepare about 1 mg of membrane proteins in 10 min and one 2-litre column for larger amounts (up to 200 mg in 15 min). The optimal pH and phosphate concentration for the separation of hemoglobin from the membranes were found to be 7.5 and 5 mM, respectively. Sodium dodecyl sulphate (SDS) electrophoretic analysis of the membrane proteins prepared by centrifugation and by this new method shows similar protein compositions.

Sepharose

Differential centrifugation

Sodium dodecyl sulfate

10.1080/00327488008061719

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Citations (21)

Continuous Beds for Microchromatography: Cation-Exchange Chromatography

Analytical Biochemistry (1994)

Yanzhong Li Jiali Liao Kenichi Nakazato Mohammad Javed Ansari Lars Terenius

Frit

Theoretical plate

Van Deemter equation

Monolithic HPLC column

10.1006/abio.1994.1561

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Citations (65)

Selective solubilization with tween 20 of membrane proteins from Acholeplasma laidlawii

Biochimica et Biophysica Acta (BBA) - Biomembranes (1972)

Stellan Hjertén Karl‐Erik Johansson

Sodium dodecyl sulfate

Residue (chemistry)

10.1016/0005-2736(72)90252-0

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Citations (63)

Hydrophobic-interaction chromatography of proteins on continuous beds derivatized with isopropyl groups

Journal of Chromatography A (1996)

Cheng‐Ming Zeng Jiali Liao Kenichi Nakazato Stellan Hjertén

Isopropyl

Isopropyl alcohol

10.1016/s0021-9673(96)00550-x

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Citations (61)

Protein concentration and recovery from gel slabs by displacement electrophoresis (isotachophoresis) and the effects of electroosmosis and counter flow

Electrophoresis (1981)

Lars‐Göran Öfverstedt Gunnar Johansson Gunnar Fröman Stellan Hjertén

Abstract Alternative technical solutions of the concentration of protein samples or the recovery of proteins from gel slabs by displacement electrophoresis are demonstrated. The samples are collected at a boundary between high‐mobility leading ion and a low‐mobility terminating ion either in a small Sephadex G‐25 columns or in free solution in a rotating‐tube free electrophoresis apparatus. The boundary is kept stationary during electrophoresis by a counter flow of leading solution. Spacers and colored markers can be used to facilitate the collection of the proteins. Investigations showed that electroomosis is a very local phenomenon and that, as expected, the magnitude of the effects depends on the conductivity (field strength) of the solution. This implies that electroomosis will vary among different zones in a discontinuous system (as in displacement electrophoresis). Therefore, in most experiments om free solution it is very advantageous to arrange the system such that electrophoresis does not occur.

Isotachophoresis

Free-flow electrophoresis

10.1002/elps.1150020308

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Citations (41)

High-performance adsorption chromatography of transfer ribonucleic acids and proteins on 2-μm spherical beads of hydroxyapatite

Journal of Chromatography A (1990)

Johan Lindeberg Tasanee Srichaiyo Stellan Hjertén

10.1016/s0021-9673(00)96970-x

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Citations (7)

Hydrophobic interaction chromatography of incompletely methylated transfer RNA from escherichia coli on octyl-sepharose