Brushite purified phytochrome from Avena sativa L. cv. Sol II was bound to phenyl Sepharose, octyl Sepharose, CNBr‐activated Sepharose and to anti‐phytochrome immunoglobulins immobilized on Sepharose. The spectral properties of phytochrome bound to anti‐phytochrome immunoglobulins and to phenyl Sepharose were similar to phytochrome in solution. Phytochrome bound to CNBr‐activated Sepharose or to octyl Sepharose showed reduced Pfr formation after red irradiation. The reversal to Pr with far‐red light was only partial but a further increase at 667 nm took place slowly in the dark. A peak at 657 nm was seen in the difference spectrum between CNBr‐activated Sepharose‐bound phytochrome kept in darkness and the identical sample immediately after a far‐red irradiation.