Abstract
A new procedure is presented for the isolation of electron microscopically clean melanosomes. The procedure provides melanosomes which have been stripped of their membrane components so that only matrix elements are examined. Solubilization of these melanosomes is by 8 M urea‐1% Triton X‐100 treatment with reduction and alkylation. The proteins are examined on sodium dodecyl sulfate‐polyacrylamide gels and on acid‐urea polyacrylamide gels. Evidence is presented indicating the presence of four low‐molecular‐weight proteins which have not previously been reported. Data indicate that these proteins are the major components of the melanosome matrix, that they are not histones and that at least one of them is a glycoprotein.