Die trägerfreie kontinuierliche Elektrophorese und ihre Anwendung

Hannig, Kurt

doi:10.1007/bf00466586

Cited by 198 publications

(76 citation statements)

References 7 publications

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“…Step 3 : The apparatus for carrier-free electrophoresis devcloped by Hannig [28] was used (Model VAPI of Bender und Hobein, Munchen). The medium used was Tris C1 buffer, pH 6.5 (buffer in the separating chamber 2 g Tris/l, electrode buffer 8.5 g Tris/l).…”

Section: Procedures For Purifying the Aspergillopeptidasementioning

confidence: 99%

A Collagenolytic Enzyme from Aspergillus oryzae

Nordwig¹,

Jahn²

1968

European Journal of Biochemistry

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1.A highly purified protease has been prepared from culture filtrates of Aspergillus oqzae. The process consists of four steps, namely the dialysis of the starting material, precipitation with acetone, separation by carrier-free electrophoresis and fractionation with acetone. The specific activity of the protease is increased 40 times or more. The product was shown to be a single substance by means of the ultracentrifuge, disc electrophoresis and immuno-electrophoresis. As far as investigated, it is free of non-specific activities.2 . The molecular weight was found to be about 20,000 by elution from a Sephadex 0-75 column, by ultracenttrifugation and by amino acid analysis. The pH optimum normally lies between 9 and 10. The protease cannot be activated with metal ions; it is, however, inhibited by Cuzf, Hg2+ and Zn2+ ions. It is also inhibited by di-isopropyl phosphofluoridate and other compounds that react specifically with serine.3. The protease splits denatured proteins preferentially, but not solely, a t the peptide bonds of amino acids with acid side chains as shown by investigations on long-chain model peptides. It also digests native collagen. The mode of splitting is the same as that by which the collagenase from Clostridium histolyticum splits the apolar regions. However, bonds involving hydroxyproline appear to be resistant to attack by the Aspergillus enzyme. I n addition, the prot,ease described here is capable of digesting bonds of the polar regions of the native collagen molecule. The protease also acts as an esterase. 4.On the basis of the various types of proteolytic specificity found for the protease a new concept is put forward for understanding collagen breakdown in vivo and in vitro.

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Section: Procedures For Purifying the Aspergillopeptidasementioning

confidence: 99%

A Collagenolytic Enzyme from Aspergillus oryzae

Nordwig¹,

Jahn²

1968

European Journal of Biochemistry

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“…Barrolier's method using very thin, flat layers 22 has particularly been developed by Hannig 23 who reports separation of human and rabbit erythrocytes), 23 and also used by Wolfgang 24 (in whose method the sample is in contact with paper for a short time).…”

Section: I·'mentioning

confidence: 99%

“…(31) constant; Eq. (23) vertical height of main migration chamber; Eq. (3); .. absolute viscosity; Eq.…”

Section: ~(mentioning

confidence: 99%

Stable-Flow Free-Boundary Migration and Fractionation of Cell Mixtures: Sedimentation and Electrophoresis

Mel¹

1963

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“…1,2 In FFE, a thin sheath of laminar flow is introduced perpendicular to the direction of the applied electric field (Figure 1), which affects the position of charged particles or solutes. Since the separated samples flow with the fluid field, this technique is capable of separating and collecting analytes continuously.…”

Section: Introductionmentioning

confidence: 99%

Mathematical and numerical model to study two-dimensional free flow isoelectric focusing

et al. 2014

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Even though isoelectric focusing (IEF) is a very useful technique for sample concentration and separation, it is challenging to extract separated samples for further processing. Moreover, the continuous sample concentration and separation are not possible in the conventional IEF. To overcome these challenges, free flow IEF (FFIEF) is introduced in which a flow field is applied in the direction perpendicular to the applied electric field. In this study, a mathematical model is developed for FFIEF to understand the roles of flow and electric fields for efficient design of microfluidic chip for continuous separation of proteins from an initial well mixed solution. A finite volume based numerical scheme is implemented to simulate two dimensional FFIEF in a microfluidic chip. Simulation results indicate that a pH gradient forms as samples flow downstream and this pH profile agrees well with experimental results validating our model. In addition, our simulation results predict the experimental behavior of pI markers in a FFIEF microchip. This numerical model is used to predict the separation behavior of two proteins (serum albumin and cardiac troponin I) in a two-dimensional straight microchip. The effect of electric field is investigated for continuous separation of proteins. Moreover, a new channel design is presented to increase the separation resolution by introducing cross-stream flow velocity. Numerical results indicate that the separation resolution can be improved by three folds in this new design compare to the conventional straight channel design. V C 2014 AIP Publishing LLC.

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Die trägerfreie kontinuierliche Elektrophorese und ihre Anwendung

Cited by 198 publications

References 7 publications

A Collagenolytic Enzyme from Aspergillus oryzae

A Collagenolytic Enzyme from Aspergillus oryzae

Stable-Flow Free-Boundary Migration and Fractionation of Cell Mixtures: Sedimentation and Electrophoresis

Mathematical and numerical model to study two-dimensional free flow isoelectric focusing

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