title: Interconversion of active and inactive forms of phosphorylase and glycogen synthetase in oocytes and embryos of the loach (Misgurnus fossilis L.).
abstract: Glycogen synthetase (EC 2.4.1.11) from oocytes and embryos of the loach (Misgurnus fossilis L.) has been found only in the D-form. The intensive glycogen accumulation during oogenesis did not correspond with the glycogen synthetase interconversion in the I-form.In isolated oocytes and embryos of the loach insulin transforms glycogen synthetase into the form which is desensitized for ATP inhibition. Insulin treatment enhancesVmaxwithout affecting theKm(UDP-glucose) only with an excess of activator-glucose-6-P. Simultaneously insulin treatment converts the phosphorylase (EC 2.4.1.1.) into the latent form.
authors.affiliation: Institute of Developmental Biology, Academy of Sciences of the USSR, Moscow.
authors.forename: Yu G
authors.initials: YG
authors.lastname: Yurowitzky
authors.affiliation: Institute of Developmental Biology, Academy of Sciences of the USSR, Moscow.
authors.forename: L S
authors.initials: LS
authors.lastname: Milman