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Title: EFFECT OF FATTY ACID ON THE IODINATION OF BOVINE SERUM ALBUMIN

Journal Article · · Journal of Molecular Biology (England)

The influence of the presence of stearic acid bound to bovine serum albumin (BSA) on the iodination of the protein with I/sup 125/ and I/sup 131/ was investigated. Defatted BSA (0.2 mu mole) was dissolved in 0.8 ml 0.2M Na/sub 2/ HPO/sub 4/ and this was added to 0.4 mu mole stearic acid in 10 mu l absolute ethanol. The solution was allowed to stand until it had become completely clear, or about 30 min. The solution was then mixed with 0,5 ml (1.65 mu atom I) of the stock rodine monochloride solution containing 2 mu C I/sup 131//ml. The pH of the resulting reaction mixture was 7.7. After 10 min. at room temperature, the iodinated protein was precipitated by the addition of 0.4 ml of a trichloroacetic acid-mercaptoethanol-NaI solution. The precipitates were washed, then subjected to partial acid hydrolysis at 37 deg C in concentrated HCl. The hydrolysates were examined by paper electrophoresis followed by radioautography. Qualitatively identical patterns were obtained at the level of 4 and 7 atoms I incorporated per mole BSA. A number of additional peptides are present in the hydrolysate of serum albumin iodinated in presence of fatty acid as compared with the hydrolysate of the iodinated defatted protein. The data suggested that the binding of 2 moles of stearic acid to defatted BSA is associated with a conformational rearrangement resulting in the accessibility of a greater number of tyrosine residues to iodination. (TCO)

Research Organization:
Lab. of Molecular Biology, Cambridge, Eng.
Sponsoring Organization:
USDOE
NSA Number:
NSA-18-011596
OSTI ID:
4107700
Journal Information:
Journal of Molecular Biology (England), Vol. Vol: 7; Other Information: Orig. Receipt Date: 31-DEC-64
Country of Publication:
Country unknown/Code not available
Language:
English