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A method is described for isolation of insulin from chicken pancreas which makes use of modifications of established procedures to deal with the low insulin content of the tissue and permits isolation of significant quantities of the hormone. The insulin isolated is essentially homogeneous by paper chromatography and polyacrylamide gel electrophoresis. The amino acid composition of the insulin and of the separated A and B chains is consistent with the known amino acid sequence of chicken insulin. (Endocrinology 83: 1323, 1968)
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Kimmel et al. (1968) studied this question.
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