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PMID: 6458491 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Partial proteolysis of human L-type phosphofructokinase.

Enzyme ·Vol. 26 ·No. 6 ·1981-00-00 ·Pages 315-20

Lagrange JL, Meienhofer MC, Kahn A

Abstract

L (liver) type phosphofructokinase subunits purified from human leukocytes are slightly lighter than L subunits from liver and red blood cells. A mild treatment of red blood cell L4 enzyme with subtilisin converts its subunits into forms of similar molecular weight to leukocyte enzyme. From a kinetical point of view, subtilisin-treated L4 phosphofructokinase and leukocyte enzymes are characterized by a decrease of the allosteric properties as compared to non-treated red cell L4 phosphofructokinase.

MeSH Terms
Adult Catalysis Enzyme Activation Humans Kinetics Leukocytes/enzymology Liver/enzymology Molecular Weight Phosphofructokinase-1/antagonists & inhibitors,metabolism
Chemicals
Phosphofructokinase-1
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Lagrange J L
Meienhofer M C
Kahn A
Article Info
Journal
Enzyme
Abbr.
Enzyme
ISSN
0013-9432
Published
1981-00-00
Pages
315-20
Language
English
Region
Switzerland
NLM ID
1262265
Subset
IM
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