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

<p>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.</p>

Name thesis:degree_name

Doctor of Philosophy (PhD)

Level thesis:degree_level

Thesis

Year

1986

Author dc:creator

• Fantl, Wendy Jane

Contributors dc:contributor

• James Manning

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

Repository record dc:identifier

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

OAI identifier oai:identifier

oai:digitalcommons.rockefeller.edu:student_theses_and_dissertations-1484