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High Pressure Fosters Protein Refolding from Aggregates at High Concentrations

High Pressure Fosters Protein Refolding from Aggregates at High Concentrations

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_citationtrail_10_1073_pnas_96_23_13029

High Pressure Fosters Protein Refolding from Aggregates at High Concentrations

About this item

Full title

High Pressure Fosters Protein Refolding from Aggregates at High Concentrations

Publisher

United States: National Academy of Sciences of the United States of America

Journal title

Proceedings of the National Academy of Sciences - PNAS, 1999-11, Vol.96 (23), p.13029-13033

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences of the United States of America

More information

Scope and Contents

Contents

High hydrostatic pressures (1-2 kbar), combined with low, nondenaturing concentrations of guanidine hydrochloride (GdmHCl) foster disaggregation and refolding of denatured and aggregated human growth hormone and lysozyme, and β -lactamase inclusion bodies. One hundred percent recovery of properly folded protein can be obtained by applying pressures...

Alternative Titles

Full title

High Pressure Fosters Protein Refolding from Aggregates at High Concentrations

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_crossref_citationtrail_10_1073_pnas_96_23_13029

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_citationtrail_10_1073_pnas_96_23_13029

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.96.23.13029

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