Abstract
Isolated phytochrome was demonstrated to be free from all but trace impurities by high speed velocity and equilibrium ultracentrifugation, polyacrylamide electrophoresis, and gel filtration in Sephadex G-200. The results from these techniques and from electron microscopy, amino acid analyses, and tryptic peptide separations were consistent with the native phytochrome molecules existing as 14-S hexamers and 9-S tetramers of 2-S monomer units. The monomer unit appears to be chemically identical, existing as a single polypeptide chain of approx. 42 000 molecular weight. These monomer units appear to be associated through noncovalent type bonds. Fluorescence studies indicated that when the 660 nm-absorbing form of phytochrome was excited at 290 nm, it fluoresced intensely at 340 nm and slightly at 672 nm. When excited at 370 nm, it fluoresced at 672 nm.
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