Abstract
Paper chromatographic and acid hydrolysis techniques were used to determine the chemical nature of nine ninhydrin-positive protein constituents from fresh tissue homogenates. The techniques, which are described in detail, included both one-way and two-way chromatograms. The nine constituents found, and/or the amino acids yielded by their acid hydrolysis, were: glutamic acid, serine, and an unknown compound; glutamic acid and alanine; threonine, serine, and beta alanine; aspartic acid and serine; alanine and tyrosine; proline; tryptophan, phenylalanine (?), and valine; methionine and valine. It was concluded that most of the constituents are probably simple peptides (though the Biuret test did not give typical results), and that one constituent is the free amino acid proline.
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