Premium
Localization of pyruvate kinase isozymes in bovine kidney and comparison of these patterns with those of lactate dehydrogenases and aldolases
Author(s) -
Cardenas Janet M.,
Richards Thomas C.,
Gabourel Linda
Publication year - 1978
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040960207
Subject(s) - isozyme , pyruvate kinase , gluconeogenesis , pkm2 , biochemistry , aldolase a , pyruvate dehydrogenase lipoamide kinase isozyme 1 , pyruvate dehydrogenase phosphatase , biology , lactate dehydrogenase , glycolysis , microbiology and biotechnology , kidney , pyruvate dehydrogenase kinase , immunofluorescence , enzyme , pyruvate dehydrogenase complex , antibody , endocrinology , immunology
Electrophoretic and immunofluorescence analysis were used to study the distribution of pyruvate kinase isozymes in the bovine kidney. Electrophoretic analysis demonstrated the presence of large amounts of K 4 plus small amounts of K‐M hybrids in cortical, medullary, and papillary sections cut from the kidney. Nearly all of the K‐L hybrids seen in whole kidney extracts were found in cortical sections. Immunofluorescence of frozen sections revealed the presence of type L subunits in the tubules but the complete absence of this subunit type in glomeruli. Glomeruli do contain large quantities of pyruvate kinase isozymes, probably K 4 and K‐M hybrids, that cross‐react with antibodies produced against type M pyruvate kinase. Type L‐containing forms of pyruvate kinase and aldolase type B both appear to be found in cell types thought to be capable of catalyzing gluconeogenesis, while type K pyruvate kinase and type A aldolase are found in predominantly glycolytic cell types of the kidney. Lactate dehydrogenase isozymic patterns appear to be less closely correlated with glycolytic versus gluconeogenic functions of the kidney but may be determined more directly by other metabolic functions.