{"id":{"repo_id":"rockefeller","oai_identifier":"oai:digitalcommons.rockefeller.edu:student_theses_and_dissertations-1484"},"canonical_url":"https://search.dev.ndltd.org/etd/rockefeller/oai:digitalcommons.rockefeller.edu:student_theses_and_dissertations-1484","repository":{"repo_id":"rockefeller","name":"Rockefeller","base_url":"https://digitalcommons.rockefeller.edu/do/oai/"},"display":{"title":"The Specific Carboxymethylation of the N-Terminal Amino Groups of Human Hemoglobin: Structural and Functional Implications","abstract":"<p>The studies reported in this thesis describe the conditions elucidated for the selective reductive carboxymethylation of the α-amino termini of hemoglobin (Hb)<sup>1</sup> and the structural and functional consequences of such a modification. The initial premise for such a modification (HbNHCH<sub>2</sub>COO<sup>-</sup>) was to test its usefulness as a carbon dioxide (CO<sub>2</sub>) or carbamino analogue (HbNHCOO<sup>-</sup> ). 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 CO<sub>2</sub> to Hb as well as the interplay between this effector and other important physiological modulators of hemoglobin.</p>","abstract_html":"&lt;p&gt;The studies reported in this thesis describe the conditions elucidated for the selective reductive carboxymethylation of the α-amino termini of hemoglobin (Hb)&lt;sup&gt;1&lt;/sup&gt; and the structural and functional consequences of such a modification. The initial premise for such a modification (HbNHCH&lt;sub&gt;2&lt;/sub&gt;COO&lt;sup&gt;-&lt;/sup&gt;) was to test its usefulness as a carbon dioxide (CO&lt;sub&gt;2&lt;/sub&gt;) or carbamino analogue (HbNHCOO&lt;sup&gt;-&lt;/sup&gt; ). 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 CO&lt;sub&gt;2&lt;/sub&gt; to Hb as well as the interplay between this effector and other important physiological modulators of hemoglobin.&lt;/p&gt;","abstract_has_math":false,"creators":["Fantl, Wendy Jane"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Thesis","degree_discipline":null,"degree_department":null,"school":null,"contributors":["James Manning"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1986,"date_issued":"1986-01-01T08:00:00Z","date_published":"1986-01-01T08:00:00Z","updated_at":"2026-07-24T04:11:51Z","subjects":["selective reductive carboxymethylation","hemoglobin modification","alpha-amino termini","carbon dioxide binding","carbamino analogue","physiological modulators","Life Sciences"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://digitalcommons.rockefeller.edu/student_theses_and_dissertations/480","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["James Manning"]},{"key":"dc:creator","label":"Author","values":["Fantl, Wendy Jane"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["selective reductive carboxymethylation","hemoglobin modification","alpha-amino termini","carbon dioxide binding","carbamino analogue","physiological modulators","Life Sciences"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://digitalcommons.rockefeller.edu/student_theses_and_dissertations/480"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["<p>The studies reported in this thesis describe the conditions elucidated for the selective reductive carboxymethylation of the α-amino termini of hemoglobin (Hb)<sup>1</sup> and the structural and functional consequences of such a modification. The initial premise for such a modification (HbNHCH<sub>2</sub>COO<sup>-</sup>) was to test its usefulness as a carbon dioxide (CO<sub>2</sub>) or carbamino analogue (HbNHCOO<sup>-</sup> ). 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 CO<sub>2</sub> to Hb as well as the interplay between this effector and other important physiological modulators of hemoglobin.</p>"]},{"key":"dc:title","label":"Title","values":["The Specific Carboxymethylation of the N-Terminal Amino Groups of Human Hemoglobin: Structural and Functional Implications"]}]}],"canonical_facts":{"dc:contributor":["James Manning"],"dc:creator":["Fantl, Wendy Jane"],"dc:description.abstract":["<p>The studies reported in this thesis describe the conditions elucidated for the selective reductive carboxymethylation of the α-amino termini of hemoglobin (Hb)<sup>1</sup> and the structural and functional consequences of such a modification. The initial premise for such a modification (HbNHCH<sub>2</sub>COO<sup>-</sup>) was to test its usefulness as a carbon dioxide (CO<sub>2</sub>) or carbamino analogue (HbNHCOO<sup>-</sup> ). 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 CO<sub>2</sub> to Hb as well as the interplay between this effector and other important physiological modulators of hemoglobin.</p>"],"dc:identifier":["https://digitalcommons.rockefeller.edu/student_theses_and_dissertations/480"],"dc:subject":["selective reductive carboxymethylation","hemoglobin modification","alpha-amino termini","carbon dioxide binding","carbamino analogue","physiological modulators","Life Sciences"],"dc:title":["The Specific Carboxymethylation of the N-Terminal Amino Groups of Human Hemoglobin: Structural and Functional Implications"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Doctor of Philosophy (PhD)"]},"updated_at":"2026-07-24T04:11:51Z"}