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Cellular retinoic acid-binding protein from rat testis. Purification and characterization
The Journal of Biological Chemistry
|July 10, 1978
Summary
Researchers purified cellular retinoic acid-binding protein from rat testes, finding it binds retinoic acid with high affinity. This purified protein is crucial for understanding retinoid metabolism and function in reproductive tissues.
Area of Science:
- Biochemistry
- Molecular Biology
- Reproductive Biology
Background:
- Cellular retinoic acid-binding protein (CRABP) plays a role in retinoid metabolism.
- Understanding CRABP's properties is essential for studying its biological functions.
Purpose of the Study:
- To purify cellular retinoic acid-binding protein (CRABP) from rat testes.
- To characterize the physical and binding properties of purified CRABP.
Main Methods:
- Purification involved acid precipitation, gel filtration, and DEAE-cellulose chromatography.
- Molecular weight was determined using gel filtration and SDS-PAGE.
- Binding affinity was assessed via fluorometric titration.
Main Results:
- CRABP was purified ~12,000-fold from rat testes.
- The purified protein consists of a single polypeptide chain with a molecular weight of 14,600 Da.
- CRABP exhibits high-affinity binding to retinoic acid with a K(d) of 4.2 x 10(-9) M.
Conclusions:
- Homogeneous cellular retinoic acid-binding protein (CRABP) was successfully isolated from rat testes.
- The purified CRABP demonstrates high affinity for retinoic acid, supporting its role as a carrier protein.