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Abstract

Moderate u.v.-doses (2537 Å) sufficient to reduce enzymatic activities of native enzymes up to about 90 per cent, in general do not produce measurable amounts of smaller dialyzable fragments.

The disappearance of the original boundary in sedimentation diagrams is mostly due to the formation of rapidly sedimenting polydispersed material. Generally the sedimentation constants of the native proteins are not significantly changed. The boundaries, however, often loose their symmetry. The quantum yields for the disappearance of the original boundaries are roughly inversely proportional to the molecular weights. The number of molecules disappearing from the main peak is smaller than the number of molecules inactivated by a given dose. The data indicate that ultracentrifugation provides no satisfactory method for separation of native molecules from the damaged and inactivated. Proteins with labile quaternary structures (e.g. thyroglobulin or hemocyanine) which tend to dissociate under very mild conditions show an enhanced dissociation after u. v.-irradiation.