PROPERTIES OF A PROTEIN ANTIGENICALLY RELATED TO TRYPTOPHAN SYNTHETASE INNEUROSPORA CRASSA

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Abstract
Rabbit antibody against partially purified preparations of Neurospora crassa tryptophan synthetase (Tsase) quantitatively and completely neutralizes enzyme activity, and the neutralization reaction is unaffected by substrate or pyridoxal phosphate. A mutant unable to convert indole to tryptophan and lacking Tsase produces a protein (CRM) immunologically indistinguishable from the enzyme. Tsase and CRM can be distinguished by their different stability on dialysis. Quantitative neutralization, adsorption and precipitin studies indicate that the Tsase-anti-Tsase and CRM-anti-CRM reactions can be studied as single antigen-antibody systems, so as to permit detailed immunochemical analysis of the problem of gene function and enzyme formation.