What question did this study set out to answer?

To establish a rapid and efficient purification protocol for isolating highly pure recombinant annexin V and its mutants for structural and biophysical characterization.

August 23, 1993FEBS LettersOpen Access

A rapid and efficient purification method for recombinant annexin V for biophysical studies

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Authors

ABAlexander BürgerInternational Craniofacial Institute RBRobert BerendesSyngenta (Switzerland)DVDieter VogesBiomax Informatics (Germany)

Discussion

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Implication

Experimental study demonstrates a multi-step purification protocol yielding contaminant-free recombinant annexin V, facilitating detailed biophysical and structural investigations.

Key Points

To establish a rapid and efficient purification protocol for isolating highly pure recombinant annexin V and its mutants for structural and biophysical characterization.
Released intracellular recombinant proteins via mild bacterial cell lysis using osmotic shock.
Exploited reversible calcium-mediated binding of annexin V to liposomes for selective recovery.
Conducted ion-exchange chromatography as the terminal purification step.
Recombinant annexin V eluted as a single, distinct peak during the final ion-exchange chromatography stage.
Produced isolated protein free of any detectable contaminants, suitable for single-channel measurements, X-ray crystallography, and electron microscopy.

Cite This Study

Bürger et al. (1993) studied this question.

synapsesocial.com/papers/6a8318d6c4b5dbf8331f2db0 https://doi.org/10.1016/0014-5793(93)80185-w

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August 23, 1993FEBS LettersOpen Access

A rapid and efficient purification method for recombinant annexin V for biophysical studies

View Full Paper

Ask AI

Bookmark

Authors

ABAlexander BürgerInternational Craniofacial Institute RBRobert BerendesSyngenta (Switzerland)DVDieter VogesBiomax Informatics (Germany)

Discussion

Member takes

Implication

Experimental study demonstrates a multi-step purification protocol yielding contaminant-free recombinant annexin V, facilitating detailed biophysical and structural investigations.

Key Points

To establish a rapid and efficient purification protocol for isolating highly pure recombinant annexin V and its mutants for structural and biophysical characterization.
Released intracellular recombinant proteins via mild bacterial cell lysis using osmotic shock.
Exploited reversible calcium-mediated binding of annexin V to liposomes for selective recovery.
Conducted ion-exchange chromatography as the terminal purification step.
Recombinant annexin V eluted as a single, distinct peak during the final ion-exchange chromatography stage.
Produced isolated protein free of any detectable contaminants, suitable for single-channel measurements, X-ray crystallography, and electron microscopy.

Cite This Study

Bürger et al. (1993) studied this question.

synapsesocial.com/papers/6a8318d6c4b5dbf8331f2db0 https://doi.org/10.1016/0014-5793(93)80185-w

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