ADAPTATION OF THE MOREL SISLEY PROTEIN DIAZOTIZATION PROCEDURE TO THE HISTOCHEMICAL DEMONSTRATION OF PROTEIN BOUND TYROSINE | Zendy

R. D. Lillie | Zendy

Open Access

ADAPTATION OF THE MOREL SISLEY PROTEIN DIAZOTIZATION PROCEDURE TO THE HISTOCHEMICAL DEMONSTRATION OF PROTEIN BOUND TYROSINE

Author(s) -

R. D. Lillie

Publication year - 1957

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/5.5.528

Subject(s) - tyrosine , reagent , potassium hydroxide , chemistry , amino acid , potassium , sulfonic acid , hydroxide , coupling (piping) , adaptation (eye) , biochemistry , chromatography , organic chemistry , biology , materials science , neuroscience , metallurgy

Protein diazotization followed by alkaline coupling with a naphthol has been successfully applied for the histochemical localization of the protein bound tyrosine in tissues. Prolonged nitrous acid treatment in the cold is required (18-24 hours at 3°C). The best coupling reagent so far tried is 1-amimio-8-naphthol-4-sulfonic acid (S acid) and coupling succeeds best in a 1 % potassium hydroxide in 70 % alcohol, allowing 1 to 4 hours at 3°C. Topochemical results parallel those of the Millon reactions, with greater color intensities and superior histologic definition.

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