ON THE PRESENCE OF MYOGLOBIN AND CYTOCHROME OXIDASE IN THE CARTILAGINOUS ODONTOPHORE OF THE MARINE SNAIL, BUSYCON

¹ The Marine Biological Laboratory, Woods Hole, Mass.; The Special Dental Research Laboratory, V. A. Hospital, Brooklyn 9, N. Y.; and the Department of Anatomy, University of Pennsylvania, School of Medicine, Philadelphia, Pa.

1. Myoglobin and cytochrome oxidase activities were shown to exist together in a cartilaginous tissue for the first time, in the odontophore of Busycon canaliculatum.

2. The absorption spectra of the cartilage myoglobin were characteristic for this class of pigments. Similarly, the absorption spectra of the pyridine hemochrome prepared from the pigment were characteristic of ferroprotoporphyrin-pyridine hemochrome.

3. The Qo₂ (dry weight basis) of cartilage homogenates, employing hydroquinone as substrate and added cytochrome c, was 9.4 in an air atmosphere at 37° C. Such homogenates were also capable of oxidizing reduced cytochrome c.