JBC INTERFERin siRNA transfection reagent

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Isolation and Characterization of Bovine Thyrocalcitonin

H. Bryan Brewer Jr. 1, Robert J. Schlueter 2, and J. P. Aldred 2

From the 1 From the Molecular Disease Branch, National Heart and Lung Institute, National Institutes of Health, Bethesda, Maryland 20014
2 From the Departments of Biochemistry and Pharmacology, Armour Pharmaceutical Company, Kankakee, Illinois 60901

Bovine thyrocalcitonin has been isolated in homogeneous form following a 40,000-fold purification. The isolated hormone contains 32 amino acids including Arg1, His1, Thr2, Ser4, Glu1, Pro2, Gly3, Ala1, Val1, Met1, Asn3, Asp1, Lys1, Tyr2, Phe2, Leu3, Trp1, Cys2. The purified peptide is resolved by chromatography on cellulose thin layer plates or carboxymethyl cellulose into two components. These two components differ in the oxidative state of the methionine residue; however, both forms have an equal biological activity of 200 Medical Research Council units per mg. The amino acid composition of the bovine hormone differs from the porcine by 3 residues, the human by 18, and salmon by 16.

Submitted on March 4, 1970


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