Iodination-induced alterations in biochemical properties of human placental insulin receptor
- 16 November 1987
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 224 (1) , 198-200
- https://doi.org/10.1016/0014-5793(87)80447-7
Abstract
Insulin receptors from human placenta have been labeled by using an oxidative iodination procedure (iodogen-mediated or chloramine-T-mediated), Bolton-Hunter reagent or [3H]acetic anhydride. The oxidative iodination procedure reduces the affinity for 131I-insulin and the receptor protein becomes fragmented into smaller pieces with an S20,w value of 5–6. However, treatment with Bolton-Hunter reagent or [3H]acetic anhydride does not alter the Kd of 131I-insulin binding and the S20,w value remains unchanged with respect to the native receptor. It is proposed that for labeling multisubunit sulfhydryl-linked protein drastic oxidative iodination procedures should be avoidedKeywords
This publication has 2 references indexed in Scilit:
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