Preparation of Pure Proteins From Hog Thyroid Glands by Column Chromatography on Diethylaminoethylcellulose

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Abstract
Saline extracts of hog thyroid glands were chromatographed on columns of diethylaminoethyl (DEAE)-cellulose using gradients of pH and salt concentration. Two major peaks of protein emerged from these columns. When rechromatographed under identical conditions, part of the first peak to emerge from the column redistributed itself to give two peaks which appeared in positions corresponding to those of the two peaks eluted from the first chromatographic run. Examination of the ultracentrifugal components had taken place during chromatography on DEAE-cellulose. After further purification by a run in the separation cell, about 96% of the sedimentary material was located in the peak with S20 w = 18. Most such runs gave even higher purity. Quantitative paper chromatography of the iodoamino acids of an enzymic hydrolysate of protein from the first peak and from three parts of a broad second peak eluted from a column of DEAE-cellulose indicated that the ratio of iodotyrosines to iodothyronines was 1.9, 3.7, 4.2, and 8.8, respectively.

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