Abstract
A radioiodination method using bovine lactoperoxidase covalently coupled with Sepharose-4B, was successfully applied to a-amylase. Unlike some chemical iodination procedures, the lactoperoxidase method appeared to be quite gentle, employing only 5—10 NaI and traces of hydrogen peroxide as oxidising agent. The catalytic activity of the labelled enzyme appeared to depend on the total iodide to amylase molar ratio. Ratios greater than 0.6 reduced the catalytic activity. There was no loss of enzyme activity when iodinated at ratios up to 0.6. Amylase labelled under these conditions appeared suitable for metabolic studies. When canine plasma amylase concentration was artificially raised (5—10-fold), the disappearance curves of radioactivity and amylase activity were parallel. Tracer studies in dogs are also described.
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