1. Three azo-dye-binding proteins were identified in the soluble cell supernatant fraction from livers of rats that had received 4-dimethylaminoazobenzene by intraperitoneal injection. 2. One is basic and was highly purified. It has an isoelectric point of pH8.4 in barbital-sodium chloride buffer, I0.1, an S(20,w) value of 3.5s and a molecular weight determined by Sephadex chromatography of 45000. 3. It does not have N-terminal amino acids with free alpha-amino groups. 4. Digestion with Pronase gives rise to a single azo-dye-bound peptide, which on hydrolysis is shown to contain glycine, alanine, serine, threonine, glutamic acid and aspartic acid. The amino acid that binds the azo-dye was not identified. 5. On starch-gel electrophoresis the basic protein separates into a double band, indicating microheterogeneity. 6. The other two proteins were partially purified and occur in a fraction together. They have isoelectric points near neutrality and a molecular weight as determined by Sephadex chromatography of 13800. 7. The absorption spectra in formic acid of both the basic and the low-molecular-weight proteins are similar. The azonium ion has an absorption maximum at 518mmu and another adsorbed chromogen is present with an absorption maximum at 395mmu.

1. Changes in the structure and function of the rough-surfaced endoplasmic reticulum of the rat liver as deduced by electron microscopy, polysome analysis and the amino acid-incorporating activity of microsome fractions have been followed at various time-intervals after a single intraperitoneal dose of the hepatocarcinogen 4-dimethylaminoazobenzene. 2. The earliest effect observed was detachment of polysomes and disorganization and vesiculation of the cisternae of the roughsurfaced endoplasmic reticulum. This occurred after 6hr. 3. Subsequent to this was a phase of polysome disaggregation accompanied by impaired amino acidincorporating activity by microsomes together with a much enhanced stimulating effect of polyuridylic acid on amino acid uptake. This reached a maximum at 24hr. 4. By 40hr. polysomes had re-formed and the amino acid-incorporating activity, together with the polyuridylic acid effect, were similar to those in controls. 5. It was not until 1 2 hr. that something like the normal structure of the rough-surfaced endoplasmic reticulum was re-established. 6. It is not yet possible to relate these changes specifically with the process of azo-dye carcinogenesis.

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