Cited by 497Hemoglobin structure and functionProtein purification and stabilityBlood properties and coagulation

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PROTEIN COAGULATION AND ITS REVERSAL

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Anson, M. L., Mirsky, A. E.·1930·Journal of General Physiology

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Abstract

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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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
DOI: 10.1085/jgp.13.4.469
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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PROTEIN COAGULATION AND ITS REVERSAL

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