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Studies have been carried out on the protein solubility profile of Kulthi (Macrotylona uniflorus, Lam.) seed in aqueous solution over various pHs and at different concentrations of NaCl, Na2SO3, CaCl2, and MgCl2 at pH 8.0. Amino acid analysis of isolated protein identified 17 amino acids, 9 of which are essential. Gel-permeation chromatography on Sephadex G-200 revealed the presence of seven components in the protein fraction. Their molecular weights were determined by two comparable standard methods. Extractable Kulthi seed proteins in salt solutions were separated electrophoretically into eight fractions whose molecular weights were found to be 186,200, 131,800, 108,400, 91,200, 53,700, 44,700, 38,000, and 27,500.

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A spray reagent for easy identification of amino acids on thin-layer chromatography plates has been introduced. The reagent is capable of developing various distinguishable colours with many of them. A probable mechanism for such colour formation has also been proposed.

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