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Related Concept Videos

Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
Drug Binding to Blood Components01:30

Drug Binding to Blood Components

When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are further...
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

Phase II Reactions: Sulfation and Conjugation with α-Amino Acids

Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme activation, sulfur...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

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Related Experiment Video

Updated: Jun 22, 2026

Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications
09:24

Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications

Published on: May 8, 2026

Solid phase pegylation of hemoglobin.

Xiaoyan Suo1, Chunyang Zheng, Pengzhan Yu

  • 1National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, People's Republic of China.

Artificial Cells, Blood Substitutes, and Immobilization Biotechnology
|June 16, 2009
PubMed
Summary
This summary is machine-generated.

This study introduces a novel solid-phase method for attaching polyethylene glycol (PEG) to hemoglobin, significantly improving the yield of PEGylated hemoglobin. This enhanced PEG-hemoglobin conjugate exhibits oxygen-binding properties closer to natural red blood cells.

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Surface Passivation for Single-molecule Protein Studies

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Surface Passivation for Single-molecule Protein Studies
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Surface Passivation for Single-molecule Protein Studies

Published on: April 24, 2014

Area of Science:

  • Bioconjugation Chemistry
  • Protein Modification
  • Biomaterials Science

Background:

  • Hemoglobin-based oxygen carriers (HBOCs) are explored as blood substitutes.
  • Traditional PEGylation of hemoglobin in the liquid phase suffers from low yields and suboptimal oxygen-binding characteristics.
  • Developing efficient and controlled PEGylation methods is crucial for improving HBOC efficacy.

Purpose of the Study:

  • To develop a solid-phase conjugation process for polyethylene glycol (PEG) attachment to hemoglobin.
  • To enhance the yield and oxygen-binding properties of PEGylated hemoglobin.
  • To compare the solid-phase method with conventional liquid-phase PEGylation.

Main Methods:

  • Bovine hemoglobin was adsorbed onto an ion exchange chromatography column (solid phase).
  • Succinimidyl carbonate mPEG (SC-mPEG) was introduced as the PEGylation reagent in the mobile phase.
  • Elution was performed to separate PEGylated and unPEGylated hemoglobin.
  • Analysis utilized High-Performance Size Exclusion Chromatography (HPSEC), SDS-PAGE, and Multi-Angle Laser Light Scattering (MALLS).

Main Results:

  • The solid-phase conjugation yielded 75% mono-PEGylated hemoglobin, significantly higher than the 30% yield from liquid-phase PEGylation.
  • Analysis confirmed well-defined PEGylated hemoglobin components.
  • The P(50) values of mono-PEGylated hemoglobin (19.97–20.54 mmHg) were closer to red blood cells compared to conventionally PEGylated hemoglobin.

Conclusions:

  • Solid-phase PEGylation is an effective method for producing high-yield, well-defined PEGylated hemoglobin.
  • The developed method improves oxygen-binding affinity, making it a promising approach for hemoglobin-based oxygen carriers.
  • This technique offers a significant advancement over traditional liquid-phase PEGylation for protein modification.