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

Related Theses

View more theses from the James Manning Laboratory

Keywords

selective reductive carboxymethylation, hemoglobin modification, α-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

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://digitalcommons.rockefeller.edu/student_theses_and_dissertations/480