Dissociation of phosphohistone phosphatases from canine heart

Effect of ethanol treatment on high molecular weight phosphoprotein phosphatases of rat liver.

“…A wide variety of tissues including rat liver (Brandt et al 1974;Titanji 1977) can yield this phosphatase, which is said to dephosphorylate phosphorylase a (Brandt et al 1974(Brandt et al , 1975aKobayashi et al 1975;Khandelwal et al 1976;Hsiao et al 1977), glycogen synthase D (Khandelwal et al 1976;Killilea et al 1976), phosphohistone (Kobayashi et al 1975;Khandelwal et al 1976;Hsiao et al 1977;Titanji 1977) and still other phosphoproteins (Chou et al 1977;Khoo et al 1978). With a molecular weight of 35,000 (Brandt et al 1975a;Khandelwal et al 1976), the phosphatase has been regarded to be the catalytic subunit of higher molecular weight phosphatase(s) (Brandt et al 1974), but their exact interrelationship is still obscure, since the latter has never been purified sufficiently to investigate its subunit structure.…”