Genesine, the naked autoglucosylating protein involved in glycogen bio
synthesis, was partially purified from rat liver and some of its bioch
emical properties were characterized. Its activity was strongly activa
ted by Mn2+ and two-pH optimums were obtained. UDP-C-14-Glc was the pr
eferred glucosyl donor substrate, but also UDP-C-14-Xy1 was. It was ad
ditionally found that more than one glucose was transferred to the pro
tein or to that alpha 1,4 glucan already linked to the protein from UD
P-Glc. Glucose, maltose, xylose and UDP were inhibitors of genesine ac
tivity.