Newer techniques in protein isolation and characterization.

Methods That Disrupt Cellular Organization Traditional protein separation methods, which have developed largely from research on mammalian proteins, commonly achieve resolution either by grad~al changes in pH, ionic strength, dielectric const~t, IOn composition and temperature or by changes In such forces as fluid velocity, electric potential and gravity. " The isolation of plant seed proteins may require amendments to this list. From the standpoint that separations are energy-cGntrolled processes, pressure is an obvious and potentially useful variable. Josephs and Harrington (9) have already shown that hydrostatic pressure favors the dissociation of elastin agO'reO'ates into monomers with smaller partial specific ~ol~mes. Similar methods might prove useful in dissociating some of the highly aggregated protein mixtures often encountered in plant seeds. Detailed reviews of the extensive literature dealing with the fractionation (10,11) and characterization of proteins (12-14) have been published elsewhere. This paper briefly considers some further developments in these areas of protein chemistry.