I agree Our site saves small pieces of text information (cookies) on your device in order to deliver better content and for statistical purposes. You can disable the usage of cookies by changing the settings of your browser. By browsing our website without changing the browser settings you grant us permission to store that information on your device.
Pyruvate kinase has been used in the preparation of cell free extract from BL21 CP strain of E. coli culture for highly productive cell-free protein expression. The enzyme has been used to assay the pyruvate kinase activity by incubating with eluted DAPk (Death-associated protein kinase), a serine/threonine kinase that binds and activates pyruvate kinase. It is involved in glycolysis and in gluconeogenesis. It has been used in PGM enzyme assays to determine phosphoglycerate mutase activity. It is also used to study pyruvate kinase (PK) deficiency.
Takanori Kigawa; Takashi Yabuki; Natsuko Matsuda; Takayoshi Matsuda; Rie Nakajima; Akiko Tanaka; Shigeyuki Yokoyama. Preparation of Escherichia coli cell extract for highly productive cell-free protein expression. Journal of Structural and Functional Genomics. 2004, 5,(1-2), 63-68.
I.Mor; R.Carlessi; T.Ast; E.Feinstein; A.Kimchi. Death-associated protein kinase increases glycolytic rate through binding and activation of pyruvate kinase. Oncogene. 2012, 31,(6), 683-693.