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Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source
Published on: February 7, 2013
Stroma-free hemoglobin from bovine blood
Maria Celiana P Lima1, Cristina T Andrade
1Instituto de Macromoléculas Professora Eloisa Mano, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, Rio de Janeiro, Brazil.
Summary
This study details a method for isolating pure bovine hemoglobin (HbBv) from red blood cells using ultrasound lysis and chromatography. This technique yields high concentrations of HbBv with minimal contaminants, suitable for further applications.
Area of Science:
- Biochemistry
- Biotechnology
- Protein purification
Background:
- Bovine hemoglobin (HbBv) is a valuable protein with potential applications.
- Efficient isolation and purification methods are crucial for its use.
Purpose of the Study:
- To develop an optimized protocol for the isolation and purification of bovine hemoglobin (HbBv).
- To achieve high purity HbBv with minimal contaminants.
Main Methods:
- Whole blood treated with carbon monoxide, followed by washing and centrifugation.
- Red blood cell lysis using hypotonic media and ultrasound radiation.
- Purification via thermal treatment, filtration, and anion-exchange liquid chromatography.
Main Results:
- Ultrasound lysis yielded higher HbBv concentrations and lower phospholipid contaminants compared to other methods.
- Thermal treatment effectively removed membrane proteins.
- Anion-exchange chromatography successfully eliminated phospholipids.
Conclusions:
- The developed method provides a highly efficient and effective means for purifying bovine hemoglobin.
- The resulting purified HbBv is suitable for various downstream applications due to its high purity.
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01:24Hemoglobin
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When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
01:27Oxygen 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,...