Purification of the insulin receptor from human placenta by chromatography on immobilized wheat germ lectin and receptor antibody.

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Key Points

The study aims to purify the insulin receptor from human placental tissues using chromatography techniques.
Human placental membranes labeled with Na'251 were solubilized using Triton X-100.
Chromatography was performed on a column of immobilized wheat germ lectin followed by antibody columns.
Electrophoresis and autoradiography were used to analyze the purified receptors.
Achieved approximately 20-fold purification of insulin receptor with near complete recovery.
Binding capacity increased by 20-fold after passing through antibody columns.
Identified major bands at molecular weights of 126,000 and 42,000 in purified receptors.

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Evaluates insulin receptor purification in human placental membranes, indicating improved isolation methods.

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Harrison et al. (1980) studied this question.

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