Add time:07/17/2019         Source:sciencedirect.com

A peptide, designated thymone A, was isolated from bovine thymus by a sequence of eight procedures prior to micromanipulation. Trypsin destroyed the activity indicating the absence of a non-peptidic but active component. The peptide showed essentially single spots under three conditions of electrophoresis. Analysis revealed up to 14 individual amino acids: Asp, Glu, Gly, Ala, Val, Ile, Leu, Pro, Ser, Thr, Met, Lys, Arg and His, and a composition of > 68–71 amino acids (MW 7291–7677). The MW by behavior over Bio-Gel P-6 was ca. 8000. A level between 10–100 ng of thymone A stimulated incorporation of [3H]-thymidine into DNA; a level of 1 μg (lower?) stimulated the synthesis of cAMP. Thymone A may have functional activity or be an active pro-hormone.

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