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Evidence for phosphorylation of yeast phosphofructokinase
Author(s) -
Huse Klaus,
Jergil Bengt,
Schwidop Wolf-Dieter,
Kopperschläger Gerhard
Publication year - 1988
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(88)81330-9
Subject(s) - phosphofructokinase , phosphorylation , yeast , chemistry , biochemistry , microbiology and biotechnology , glycolysis , biology , enzyme
Radioactively labelled material from yeast cells grown in the presence of [ 32 P]phosphate was specifically recognized by antibodies raised against yeast phosphofructokinase. Purified yeast phosphofructokinase was phosphorylated in a cyclic AMP‐independent manner by a protein kinase enriched from yeast extracts. This phosphorylation occurred specifically on the β‐subunit, and 0.56 mol of phosphate/mol of subunit was incorporated. The results indicate the phosphorylation of yeast phosphofructokinase both in vivo and in vitro. Phosphofructokinase phosphorylated in vitro was more stable against proteolytic degradation compared to the non‐phosphorylated enzyme.