Gross Structure of Hæmoglobin A3 and the Nature of its Binding to Chromium-51

Journal Article · Sat Feb 02 04:00:00 EST 1963 · Nature (London)

DOI:https://doi.org/10.1038/197472a0· OSTI ID:4750651

PEARSON, H. A.; VAN METRE, M. T.; VERTREES, K. M.

The nature of the binding of Cr⁵¹ by the three fractions of hemoglobin was investigated. Starch block electrophoresis was used for the separation of hemoglobin fractions. The relation of radioactivity to protein fractions was determined in hemoglobin labeled with Cr⁵¹. It was concluded that the increased activity of Cr⁵¹ observed in the hemoglobin A₃ fraction after electrophoresis at alkaline pH is not due to a polypeptide configuration but to anodal migration of hemoglobin molecules tagged with Cr⁵¹.

• Research Organization: National Naval Medical Center, Bethesda, Md.
• Sponsoring Organization: USDOE
• NSA Number: NSA-17-013943
• OSTI ID: 4750651
• Journal Information: Nature (London), Journal Name: Nature (London) Journal Issue: 4866 Vol. 197; ISSN 0028-0836
• Publisher: Nature Publishing Group
• Country of Publication: Country unknown/Code not available
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ACIDITY
CHROMIUM 51
ELECTROPHORESIS
HEMOGLOBIN
LABELLED COMPOUNDS
MEASURED VALUES
RADIOACTIVITY