The Specific Carboxymethylation of the N-Terminal Amino Groups of Human Hemoglobin: Structural and Functional Implications

Author

Wendy Jane Fantl

Date of Award

1986

Document Type

Thesis

Degree Name

Doctor of Philosophy (PhD)

Thesis Advisor

James Manning

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View more theses from the James Manning Laboratory

Keywords

selective reductive carboxymethylation, hemoglobin modification, alpha-amino termini, carbon dioxide binding, carbamino analogue, physiological modulators

Abstract

The studies reported in this thesis describe the conditions elucidated for the selective reductive carboxymethylation of the α-amino termini of hemoglobin (Hb)¹ and the structural and functional consequences of such a modification. The initial premise for such a modification (HbNHCH₂COO^-) was to test its usefulness as a carbon dioxide (CO₂) or carbamino analogue (HbNHCOO^- ). The latter compound is formed reversibly (which is physiologically necessary) and cannot be isolated. The former is irreversibly formed and, when prepared in sufficient amounts, could lead to a wealth of information concerning the binding of CO₂ to Hb as well as the interplay between this effector and other important physiological modulators of hemoglobin.

Comments

A thesis presented to the faculty of The Rockefeller University in partial fulfillment of the requirements for the degree of Doctor of Philosophy

DOI

10.48496/67hc-3052

License and Reuse Information

This work is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 4.0 International License.

Recommended Citation

Fantl, Wendy Jane, "The Specific Carboxymethylation of the N-Terminal Amino Groups of Human Hemoglobin: Structural and Functional Implications" (1986). Student Theses and Dissertations. 480.
https://doi.org/10.48496/67hc-3052