Transferrins
[CAS# 11096-37-0]

Identification

• Classification: Biochemical >> Protein research
• Name: Transferrins
• Synonyms: Human transferrin; Holotransferrins; Muscle trophic factor
• Molecular Formula: C₁₆H₂₆N₆O₄
• Molecular Weight: 366.42
• CAS Registry Number: 11096-37-0
• EC Number: 234-318-8
• SMILES: NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC1CNCN1)NC(=O)[C@@H]1CCC(=O)N1

Properties

• Density: 1.3±0.1 g/cm³, Calc.^*
• Index of Refraction: 1.561, Calc.^*
• Boiling Point: 839.7±65.0 °C (760 mmHg), Calc.^*
• Flash Point: 461.6±34.3 °C, Calc.^*

^* Calculated using Advanced Chemistry Development (ACD/Labs) Software.

Safety Data

• Hazard Symbols: GHS07 Warning
• Risk Statements: H332
• Safety Statements: P261-P271-P304+P340-P317

Discovery and Applications

Transferrins are crucial proteins in the human body, primarily responsible for the transport of iron in the bloodstream. Discovered in the early 20th century, transferrins have since become a fundamental focus in both clinical and biochemical research due to their essential role in iron homeostasis and their implications in various health conditions.

The discovery of transferrins began with the work of early scientists who identified their role in binding and transporting iron. In the 1940s, the term "transferrin" was coined to describe this protein's function of transferring iron from one location to another within the body. Transferrins are plasma proteins that bind iron with high affinity and transport it to tissues where it is needed, particularly to the bone marrow for red blood cell production. This iron transport mechanism is vital for maintaining proper iron levels and ensuring efficient oxygen transport throughout the body.

Transferrins operate through a sophisticated mechanism involving iron binding and release. Each transferrin molecule can bind up to two iron ions. The protein binds iron in the bloodstream and transports it to cells via transferrin receptors on the cell surface. Upon binding to these receptors, the transferrin-iron complex is internalized into the cell, where iron is released and used for various cellular processes, including hemoglobin synthesis. The transferrin molecule then returns to the bloodstream to pick up more iron, ensuring a continuous supply.

The application of transferrins extends beyond their fundamental physiological role. Clinically, transferrin levels in the blood are measured as part of diagnostic tests to assess iron status and diagnose conditions such as anemia and hemochromatosis. Low transferrin levels can indicate iron deficiency anemia, while elevated levels may suggest conditions like chronic disease or iron overload.

Research into transferrins has also led to their use in therapeutic and diagnostic applications. Transferrins have been explored as delivery systems for drugs and therapeutic agents, particularly in targeted drug delivery. Their ability to bind specifically to transferrin receptors on certain cells makes them useful in targeting cancer cells or other disease sites with precision. This targeted approach minimizes damage to healthy cells and enhances the effectiveness of treatments.

Furthermore, recombinant DNA technology has enabled the production of transferrins in the laboratory, allowing for the development of transferrin-based therapies and diagnostic tools. These engineered transferrins can be used in various medical applications, including novel treatments for iron-related disorders and as components in research assays.

In summary, transferrins are indispensable proteins with a critical role in iron transport and metabolism. Their discovery has paved the way for advancements in understanding iron-related disorders and developing targeted therapeutic approaches. As research continues, transferrins remain a key area of interest, offering potential for new treatments and diagnostic innovations.

References

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