TY - JOUR
T1 - "Fluorokinase" and pyruvic kinase
AU - Tietz, Alisa
AU - Ochoa, Severo
N1 - Funding Information:
’ Aided by grants from the National Institute of Arthritis and Metabolic Diseases (Grant A-1845), U. S. Public Health Service; the Rockefeller Foundation; The American Cancer Society; and by a contract (Nonr-285 (31), NR 120-490) between the Office of Naval Research and New York Universit,y College of Medicine.
Funding Information:
2 Fellow the Jane Coffin Childs Memorial Fund for Medical Research. This investigation has been aided by a grant from the Jane Coffin Childs Memorial Fund for Medical Research.
PY - 1958/12
Y1 - 1958/12
N2 - 1. 1. The enzyme catalyzing the CO2-dependent phosphorylation of fluoride by adenosine triphosphate to yield monofluorophosphate, an activity referred to as "fluorokinase," has been isolated in crystalline form from rabbit muscle extracts. The crystalline enzyme has been found to possess considerable pyruvic kinase activity. 2. 2. A number of observations including (a) constancy of pyruvic kinase to "fluorokinase" activity ratio throughout purification and on repeated recrystallization; (b) similar ratio of the two activities for preparations purified by different methods either for pyruvic kinase or for "fluorokinase" activity; (c) requirement of K+ and same broad nucleotide specificity for the two activities (reaction with the nucleoside di- or triphosphates of adenosine, guanosine, uridine, cytidine, and inosine); and (d) inhibition of fluorophosphate formation by phosphoenolpyruvate and by pyruvate, suggest that both the pyruvic kinase and "fluorokinase" reactions are catalyzed by one and the same protein. 3. 3. The possible mechanism of the essentially irreversible "fluorokinase" reaction is discussed.
AB - 1. 1. The enzyme catalyzing the CO2-dependent phosphorylation of fluoride by adenosine triphosphate to yield monofluorophosphate, an activity referred to as "fluorokinase," has been isolated in crystalline form from rabbit muscle extracts. The crystalline enzyme has been found to possess considerable pyruvic kinase activity. 2. 2. A number of observations including (a) constancy of pyruvic kinase to "fluorokinase" activity ratio throughout purification and on repeated recrystallization; (b) similar ratio of the two activities for preparations purified by different methods either for pyruvic kinase or for "fluorokinase" activity; (c) requirement of K+ and same broad nucleotide specificity for the two activities (reaction with the nucleoside di- or triphosphates of adenosine, guanosine, uridine, cytidine, and inosine); and (d) inhibition of fluorophosphate formation by phosphoenolpyruvate and by pyruvate, suggest that both the pyruvic kinase and "fluorokinase" reactions are catalyzed by one and the same protein. 3. 3. The possible mechanism of the essentially irreversible "fluorokinase" reaction is discussed.
UR - http://www.scopus.com/inward/record.url?scp=0000686544&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(58)90372-2
DO - 10.1016/0003-9861(58)90372-2
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AN - SCOPUS:0000686544
SN - 0003-9861
VL - 78
SP - 477
EP - 493
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -