Comparative characteristics of water-soluble proteins from <Emphasis Type=Italic>Larix sibirica</Emphasis>, <Emphasis Type=Italic>Picea obovata</Emphasis>, and <Emphasis Type=Italic>Abies sibirica</Emphasis> bud meristem

The amount of water-soluble proteins in bud meristem of Larix sibirica L., Picea obovata L., and Abies sibirica L. was shown to increase by 2-3 times in autumn during development of low-temperature resistance. The fractional composition of water-soluble proteins of the studied species and the amino-acid composition of groups of water-soluble proteins with different molecular weight (MW) were similar. Nitrogen accumulated as aspartic acid, glycine, and alanine in high- and medium-molecular-weight proteins. The peptides (MW < 5 kDa) typically had a high content of hydrophobic proline and hydrophilic tyrosine.