Ps. Russouw et al., ISOLATION AND CHARACTERIZATION OF A HEAT-SOLUBLE PROTEIN FROM PEA (PISUM-SATIVUM) EMBRYOS, Seed science research, 5(3), 1995, pp. 137-144
An LEA-like protein has been isolated and characterized from pea (Pisu
m sativum) embryos. It is the most prevalent protein in a homogenate o
f pea axes heated for 10 min at 80 degrees C and then centifuged for 1
0 min at 17000 g (80 degrees C supernatant fraction). It has a molecul
ar 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. Anti
bodies to the isolated protein recognize a number of larger proteins i
n the 80 degrees C supernatant fraction of pea and other legumes (chic
k pea, soybean and bean) as well as gramineous seeds (wheat, maize and
barley). The protein undergoes a substantial increase in alpha-helica
l content at high ionic strength but does not dimerize.