MATERIALS AND METHODSTwo adenosine diphosphoglucose: a-, 4-glucan a-4-glucosyltransferases were extracted from kernels of waxy maize harvested 22 days after pollination and separated by gradient elution from a diethylaminoethyl-cellulose column. Both fractions could utilize amylopectin, amylose, glycogen, maltotriose and maltose as primers. The rate of glucose transfer from adenosine diphosphoglucose to rabbit liver glycogen of fraction II was 78% of the rate of glucose transfer to amylopectin, but with fraction I the rate of transfer of glucose to rabbit liver glycogen was 380% of that observed to amylopectin. Glucan synthesis in the absence of added primer was found in fraction I in the presence of 0.5 M sodium citrate and bovine serum albumin. The unprimed product was a methanol-precipitable glucan with principally a-1,4 linkages and some a-1,6 linkages, and its iodine spectrum was similar to that of amylopectin.Either sugar nucleotide transferases or phosphorylase could be involved in the initiation and synthesis of starch in higher plants (3,4,10,(13)(14)(15). Multiple forms of ADP-glucose:a-1,4-glucan a-4-glucosyltransferase have been separated from spinach leaves, one of which in the absence of added primer catalyzes the synthesis of a glucan with principally a-i ,4 linkages and some a-1 , 6 linkages (12). The unprimed activity was stimulated over 1000-fold by BSA3 and high concentrations of some salts (12). In maize kernels, Tsai and Nelson (15) have found evidence for the presence of multiple forms of phosphorylase, two forms of which are capable of synthesizing a polyglucan in the absence of added a-1 ,4 glucan primer.The present communication reports the existence of two forms of ADP-glucose:a-1 ,4-glucan a-4-glucosyltransferase (ADP-glucose-starch glucosyltransferase) in waxy maize, one of which can catalyze the formation of a polyglucose with properties similar to amylopectin in the absence of added primer. Rates of the unprimed reaction were up to eight times faster than the primed reaction at physiological concentrations of ADP-glucose.