Kinetics of phosphofructokinase from granulocytes isolated from patients with insulin resistance.

Abstract

Phosphofructokinases from granulocytes isolated from insulin-resistant patients, mainly those from type II diabetics where the degree of insulin resistance was more pronounced, exhibit some changes in their kinetic behavior when assayed under allosteric conditions, characterized by an increased affinity for fructose-6-phosphate, being more resistant to ATP inhibition while it became more sensitive to citrate inhibitory effect. Those changes are suggestive of a isozymic modification to a more L-type enriched enzyme with a loss of the F-type component, probably present in the normal granulocyte.

• Authors: G Campos, E Ryder, L M Morales, X Raleigh
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 185 Issue 2 Pg. 559-66 (Jun 15 1992) ISSN: 0006-291X [Print] United States
• PMID: 1535194 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Citrates
• Fructosephosphates
• fructose-6-phosphate
• Adenosine Triphosphate
• Phosphofructokinase-1

Topics

• Adenosine Triphosphate (metabolism)
• Adult
• Allosteric Regulation
• Citrates (pharmacology)
• Diabetes Mellitus, Type 1 (enzymology)
• Fructosephosphates (metabolism)
• Granulocytes (enzymology)
• Humans
• Hydrogen-Ion Concentration
• Insulin Resistance
• Kinetics
• Obesity (enzymology)
• Phosphofructokinase-1 (antagonists & inhibitors, metabolism)