ISOLATION AND CHARACTERIZATION OF A HEAT-SOLUBLE PROTEIN FROM PEA (PISUM-SATIVUM) EMBRYOS

An LEA-like protein has been isolated and characterized from pea (Pisum sativum) embryos. It is the most prevalent protein in a homogenate of pea axes heated for 10 min at 80 degrees C and then centifuged for 10 min at 17000 g (80 degrees C supernatant fraction). It has a molecular mass of 11 kDa and is very rich in hydrophilic amino acids, notably aspartate, glutamate and glycine. The protein is not recognized by an antibody to the group II dehydrin C-terminal consensus sequence. Antibodies to the isolated protein recognize a number of larger proteins in the 80 degrees C supernatant fraction of pea and other legumes (chick pea, soybean and bean) as well as gramineous seeds (wheat, maize and barley). The protein undergoes a substantial increase in alpha-helical content at high ionic strength but does not dimerize.