The enzymic hydrolysate of gluten from spelt wheat (Triticum aestivum subsp. spelta), an ancient protein-rich wheat subspecies, was subjected to repeated chromatography runs on the small pore size exclusion chromatography matrix, Biogel P-2. Two small peptide fractions were purified by rechromatography. The amino acid analyses carried out upon total hydrolysis of these fractions have shown a very high proportion of glutamic acid/glutamine, leucine, and methionine. The biological activity of the peptide fractions was tested on a model hybridoma at a concentration range from 0.02 to 0.2%. The most striking effect of peptide fractions, apparent even at the lowest concentrations tested, was a significantly higher persistence of viable cells on day 6, i.e., at the decline phase of the cultures. Culture viability values in the presence of peptide fractions were 64-74%, in comparison with 56% in the control culture. The results of this work are consistent with the concept that peptide molecules may act as antiapoptotic agents, survival factors, rather than serving as metabolic substrates.