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Preparation and characterization of (125)i labeled bovine serum albumin.

Ashwitha Rai KS - Indian J Pharm Sci (2015 Jan-Feb)

Bottom Line: Bovine serum albumin is a model protein, which has been conventionally used as protein standard and in many areas of biochemistry, pharmacology and medicine.Radioiodination procedure for bovine serum albumin employing chloramine-T as an oxidant with slight modification was evaluated critically to establish the optimal conditions for the preparation of radiolabeled tracer ((125)I-BSA) with required specific activity without impairing the immune reactivity and biological activity.Optimized radioiodination procedure involving 10 µg of chloramine-T along with 20 µg of sodium metabisulphite with 60 seconds incubation at 2° yielded (125)I-BSA with high integrity.

View Article: PubMed Central - PubMed

Affiliation: Centre for Application of Radioisotopes and Radiation Technology (CARRT), Mangalore University, Mangalagangothri-574 199, India.

ABSTRACT
Bovine serum albumin is a model protein, which has been conventionally used as protein standard and in many areas of biochemistry, pharmacology and medicine. Radioiodination procedure for bovine serum albumin employing chloramine-T as an oxidant with slight modification was evaluated critically to establish the optimal conditions for the preparation of radiolabeled tracer ((125)I-BSA) with required specific activity without impairing the immune reactivity and biological activity. Optimized radioiodination procedure involving 10 µg of chloramine-T along with 20 µg of sodium metabisulphite with 60 seconds incubation at 2° yielded (125)I-BSA with high integrity.

No MeSH data available.


Paper electrophoretic pattern of reaction mixture after radioiodination of BSA.
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Figure 4: Paper electrophoretic pattern of reaction mixture after radioiodination of BSA.

Mentions: The optimization condition was chosen and the reaction mixture was prepared. Ideally, the reaction mixture of the protein after radioiodination yields two peaks as depicted in fig. 4. The first peak corresponds to the labeled protein and the second peak corresponds to the unreacted iodide and other impurities. The fractions were collected and the yield, specific activity and radiochemical purity of the pooled fraction was determined. The yield was calculated to be around 90%. Specific activity was calculated to be 27 μCi/μg. Radiochemical purity was not less than 95%.


Preparation and characterization of (125)i labeled bovine serum albumin.

Ashwitha Rai KS - Indian J Pharm Sci (2015 Jan-Feb)

Paper electrophoretic pattern of reaction mixture after radioiodination of BSA.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4355873&req=5

Figure 4: Paper electrophoretic pattern of reaction mixture after radioiodination of BSA.
Mentions: The optimization condition was chosen and the reaction mixture was prepared. Ideally, the reaction mixture of the protein after radioiodination yields two peaks as depicted in fig. 4. The first peak corresponds to the labeled protein and the second peak corresponds to the unreacted iodide and other impurities. The fractions were collected and the yield, specific activity and radiochemical purity of the pooled fraction was determined. The yield was calculated to be around 90%. Specific activity was calculated to be 27 μCi/μg. Radiochemical purity was not less than 95%.

Bottom Line: Bovine serum albumin is a model protein, which has been conventionally used as protein standard and in many areas of biochemistry, pharmacology and medicine.Radioiodination procedure for bovine serum albumin employing chloramine-T as an oxidant with slight modification was evaluated critically to establish the optimal conditions for the preparation of radiolabeled tracer ((125)I-BSA) with required specific activity without impairing the immune reactivity and biological activity.Optimized radioiodination procedure involving 10 µg of chloramine-T along with 20 µg of sodium metabisulphite with 60 seconds incubation at 2° yielded (125)I-BSA with high integrity.

View Article: PubMed Central - PubMed

Affiliation: Centre for Application of Radioisotopes and Radiation Technology (CARRT), Mangalore University, Mangalagangothri-574 199, India.

ABSTRACT
Bovine serum albumin is a model protein, which has been conventionally used as protein standard and in many areas of biochemistry, pharmacology and medicine. Radioiodination procedure for bovine serum albumin employing chloramine-T as an oxidant with slight modification was evaluated critically to establish the optimal conditions for the preparation of radiolabeled tracer ((125)I-BSA) with required specific activity without impairing the immune reactivity and biological activity. Optimized radioiodination procedure involving 10 µg of chloramine-T along with 20 µg of sodium metabisulphite with 60 seconds incubation at 2° yielded (125)I-BSA with high integrity.

No MeSH data available.