|
|
||||||||
Clinical Chemistry, Vol 27, 906-909, Copyright © 1981 by American Association for Clinical Chemistry
RJ Edwards and DC Watts
Plasma pyruvate kinase (EC 2.7.1.40) activity contains two major isoenzymes. The "L" type originates from liver (erythrocytes contain a similar isoenzyme), the "M" type predominantly from skeletal muscle. The diagnostic use of pyruvate kinase as an index of muscle leakage requires an assay of only the M type. An M-type-selective assay for mixtures of the two isoenzymes was devised, based on the differences that the L form has a higher Km for phosphoenolpyruvate and is inhibited by about 95% by a high concentration of ADP. All relevant conditions of the assay have been examined and the reaction system has been optimized at 30 degrees C. The assay yields the expected Km values for M type pyruvate kinase. An apparent increase in activity in hemolysed plasma samples was found to be derived from leukocytes.
The following articles in journals at HighWire Press have cited this article:
![]() |
K. Jo, B. Rutten, R. C. Bunn, and D. S. Bredt Actinin-Associated LIM Protein-Deficient Mice Maintain Normal Development and Structure of Skeletal Muscle Mol. Cell. Biol., March 1, 2001; 21(5): 1682 - 1687. [Abstract] [Full Text] |
||||
![]() |
F. Duclos, V. Straub, S. A. Moore, D. P. Venzke, R. F. Hrstka, R. H. Crosbie, M. Durbeej, C. S. Lebakken, A. J. Ettinger, J. van der Meulen, et al. Progressive Muscular Dystrophy in alpha -Sarcoglycan-deficient Mice J. Cell Biol., September 21, 1998; 142(6): 1461 - 1471. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |