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Insignificance of Gluconeogenesis in Human Blood Platelets
Author(s) -
Schrijver J.,
Koster J. F.,
Hülsmann W. C.
Publication year - 1975
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/j.1365-2362.1975.tb00422.x
Subject(s) - platelet , gluconeogenesis , adenylate kinase , pyruvate kinase , biochemistry , enzyme , phosphofructokinase , chemistry , fructose , pyruvate carboxylase , adenosine diphosphate , human blood , phosphatase , medicine , endocrinology , glycolysis , biology , platelet aggregation , physiology
. Human blood platelets contain no detectable activity of the enzymes fructose diphosphatase (EC 3. 1. 3. 11), phospho‐enolpyruvate carboxykinase (EC 4. 1. 1. 32) and pyruvate carboxylase (EC 6. 4. 1. 1.). Glucose‐6‐phosphatase (EC 3. 1. 3. 9) activity is very low. Phosphofructokinase present in human blood platelets, catalyzes a reaction which can be stimulated by AMP in a platelet homogenate, due to the presence of endogenous ADP and myokinase. These enzymes are responsible for the formation of fructose‐6‐phosphate from fructose‐1, 6‐diphosphate. Pyruvate kinase (EC 2. 7. 1. 40) in human blood platelets belongs to the M‐type, which is not inhibited by ATP, at least not under the conditions applied. The results obtained indicate that gluconeogenesis in human blood platelets is not present in the way which has been established for liver and kidney.