The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Surface-Induced Denaturation of Proteins during Freezing and its Inhibition by Surfactants
Abstract
In this study, we found that the denaturation of proteins during freezing is closely related to surface-induced denaturation. Several proteins with varying sensitivities to freezing were tested, and the results were compared with susceptibilities to surface denaturation in unfrozen aqueous solution. Also, the influence of the surfactant Tween 80 on the denaturation of each of the proteins was examined during freeze-thawing, as were the effects of Tween 80 and several other surfactants on the stability of lactate dehydrogenase. Proteins formed insoluble precipitates when they were subjected to a quench cooling by dipping in liquid nitrogen, although freezing followed by supercooling caused less precipitation. A strong correlation (r = 0.99) was observed between the tendency of a protein to freeze denature and its tendency to surface denature. Also, the addition of small amounts of surface-active agents protected proteins from both freeze- and surface-induced denaturation. Freeze-induced denaturation of IL-1ra at the ice-water interface during freeze-drying was effectively prevented by adding a small amount of Tween 80. These results suggest that the denaturation of proteins during freeze-thawing can be ascribed primarily to the increase in the area of the ice-water interface during freezing.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Lactic Dehydrogenase Activity in Blood.
Wroblewski, F., & Ladue, J. S. (1955) · Experimental Biology and Medicine · doi:10.3181/00379727-90-21985 · Cited by 2,429
Protein secondary structures in water from second-derivative amide I infrared spectra
Dong, A., Huang, P., & Caughey, W. S. (1990) · Biochemistry · doi:10.1021/bi00465a022 · Cited by 1,333
Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers
Prestrelski, S. J., Tedeschi, N., Arakawa, T., & Carpenter, J. F. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81120-2 · Cited by 718
Self-citationThe mechanism of cryoprotection of proteins by solutes
Carpenter, J. F., & Crowe, J. H. (1988) · Cryobiology · doi:10.1016/0011-2240(88)90032-6 · Cited by 560
Self-citationSluzky, V, Tamada, J. A., Klibanov, A. M., & Langer, R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.21.9377 · Cited by 513
Carpenter, J. F., Prestrelski, S. J., & Arakawa, T. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1309 · Cited by 331
Self-citationProteins in frozen solutions: evidence of ice-induced partial unfolding
Strambini, G. B., & Gabellieri, E. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79640-6 · Cited by 306
Prestrelski, S. J., Arakawa, T., & Carpenter, J. F. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1310 · Cited by 225
Self-citationProtein–Solvent Interactions in Pharmaceutical Formulations
Arakawa, T., Kita, Y., & Carpenter, J. F. (1991) · Pharmaceutical Research · doi:10.1023/a:1015825027737 · Cited by 220
Self-citationvan den Berg, L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90595-8 · Cited by 119
Cited by
Protein aggregation and its inhibition in biopharmaceutics
Wang, W. (2005) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2004.11.014 · Cited by 983
Rational Design of Stable Lyophilized Protein Formulations: Some Practical Advice
Carpenter, J. F., Pikal, M. J., Chang, B. S., & Randolph, T. W. (1997) · Pharmaceutical Research · doi:10.1023/a:1012180707283 · Cited by 683
Self-citationKasper, J. C., & Friess, W. (2011) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2011.03.010 · Cited by 525
Trehalose: Current Use and Future Applications
Ohtake, S., & Wang, Y. J. (2011) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22458 · Cited by 487
Searles, J. A., Carpenter, J. F., & Randolph, T. W. (2001) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.1039 · Cited by 405
Self-citationInteractions of formulation excipients with proteins in solution and in the dried state
Ohtake, S., Kita, Y., & Arakawa, T. (2011) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2011.06.011 · Cited by 398
Shaken, Not Stirred: Mechanical Stress Testing of an IgG1 Antibody
Kiese, S., Papppenberger, A., Friess, W., & Mahler, H.-C. (2008) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.21328 · Cited by 397
Nail, S. L., Jiang, S., Chongprasert, S., & Knopp, S. A. (2002) · Pharmaceutical Biotechnology · doi:10.1007/978-1-4615-0549-5_6 · Cited by 265
White, M. R., Khan, M. M., Deredge, D., Ross, C. R., Quintyn, R., Zucconi, B. E., Wysocki, V. H., Wintrode, P. L., Wilson, G. M., & Garcin, E. D. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.618165 · Cited by 66
Metadata
- Authors
- Chang, B. S., Kendrick, B. S., & Carpenter, J. F.
- Venue
- Journal of Pharmaceutical Sciences
- Publisher
- American Geophysical Union (AGU)
- Published
- 1996-12
- Volume
- 85
- Issue
- 12
- Pages
- 1325-1330
- ISSN
- 0022-3549 (ISSN-L)
- OpenAlex
- W2066662804
- Cited by
- 476
- References
- 10
- FWCI
- 1.61
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
