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PROTEIN COAGULATION AND ITS REVERSAL
Open accessAbstract
1. By a procedure involving the use of acid acetone hemoglobin may be rapidly separated into a precipitate of denatured globin and an acetone solution of heme. 2. By neutralization procedures the denatured globin may be largely converted into a soluble, apparently native form which can combine with heme to form hemoglobin. 3. The heme may be obtained in acetone-free, slightly alkaline solution without the use of strong alkali which may modify the heme.
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“The folding paradigm stipulated that unfolded molecules will always spontaneously fold into the same shape; that is, the linear amino acid sequence specifies a protein’s folded native state.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [142]
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Linked Functions and Reciprocal Effects in Hemoglobin: A Second Look
Wyman, J. (1964) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60190-4 · Cited by 1,613
Cleavage of the haem-protein link by acid methylethylketone
Teale, F. W. J. (1959) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(59)90407-x · Cited by 1,242
Advances in protein structure prediction and design
Kuhlman, B., & Bradley, P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0163-x · Cited by 806
THE TAGGING OF RED CELLS AND PLASMA PROTEINS WITH RADIOACTIVE CHROMIUM 1
Gray, S. J., & Sterling, K. (1950) · Journal of Clinical Investigation · doi:10.1172/jci102403 · Cited by 689
Studies on the structure of hemoglobin I. Physicochemical properties of human globin
Fanelli, A. R., Antonini, E., & Caputo, A. (1958) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(58)90108-2 · Cited by 625
Metadata
- Authors
- Anson, M. L., & Mirsky, A. E.
- Affiliations
- Rockefeller University Hospital (US)
- Venue
- Journal of General Physiology
- Publisher
- Rockefeller University Press
- Published
- 1930-03-20
- Volume
- 13
- Issue
- 4
- Pages
- 469-476
- ISSN
- 0022-1295 (ISSN-L)
- 1540-7748
- PMC
- PMC2141062
- OpenAlex
- W2125550241
- Cited by
- 497
- References
- 10
- Citations by year
- 2024: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 1 · 2019: 1 · 2017: 2 · 2016: 1 · 2015: 1 · 2014: 3 · 2013: 1
- FWCI
- 10.60
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of General Physiology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Health Sciences › Medicine › Hematology › Blood properties and coagulation
- Keywords
- protein coagulation, protein denaturation, hemoglobin, globin, heme
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