Related Experiment Video
Updated: Aug 15, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
Published on: August 1, 2010
Modification of hemoglobin upon covalent coupling to dextran: enhanced stability against acid denaturation and
Abstract:
Alkylation of human hemoglobin by bromoacetylaminoethylamino-substituted dextran gave rise to a covalent dextran-hemoglobin complex with enhanced stability against acid denaturation, and reduced affinity for binding to haptoglobin, compared with free hemoglobin. These effects increased with increasing size of the dextran moiety and were not elicited by either free dextran or alkylation of hemoglobin by iodoacetamide. These observations are consistent with an inhibition by covalently attached dextran of the binding of beta-subunit of hemoglobin to haptoglobin.
More Related Videos
10:24Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
09:24Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications
Published on: May 8, 2026
Related Concept Videos
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Cooperative Allosteric Transitions
Protein Denaturation
EDTA: Chemistry and Properties
Hemoglobin
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Oxygen Transport in the Blood