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Two diverse effects of poly(L‐lysine) on rabbit skeletal muscle phosphorylase kinase: stimulation of autophosphorylation and inhibition of its activity
Author(s) -
Negami Akira,
Sakai Kuniyasu,
Kobayashi Tomoko,
Tabuchi Hikaru,
Nakamura Shun-ichi,
Yamamura Hirohei
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80107-6
Subject(s) - autophosphorylation , skeletal muscle , stimulation , lysine , chemistry , phosphorylase kinase , rabbit (cipher) , biochemistry , glycogen phosphorylase , microbiology and biotechnology , kinase , protein kinase a , enzyme , biology , endocrinology , amino acid , computer science , computer security
Polylysine greatly stimulated the autophosphorylation of phosphorylase kinase from rabbit skeletal muscle. When fully autophosphorylated, about 14 mol of phosphate per tetramer (αβγδ) were incorporated in the presence of polylysine, which was twice as much as those observed without polylysine. In contrast to this stimulatory effect of polylysine on the autophosphorylation, polylysine strongly inhibited the conversion reaction of phosphorylase b to a . The inhibition is competitive with a K i of 2.3 μg/ml. No effects of polylysine were observed on the activities of phosphorylase and cAMP‐dependent protein kinase.