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Phosphoglycerate kinase: Studies on normal and a mutant human enzyme
Author(s) -
Svirklys L. G.,
Lee C. S.,
O'Sullivan W. J.
Publication year - 1986
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01800488
Subject(s) - phosphoglycerate kinase , enzyme , biochemistry , nucleotide , biology , mutant , fraction (chemistry) , microbiology and biotechnology , enzyme assay , substrate (aquarium) , chemistry , gene , chromatography , ecology
Phosphoglycerate kinase was purified from a number of tissues obtained at autopsy from a subject with the deficiency. Properties of the mutant enzyme were compared to those of PGK purified from tissue obtained from normal subjects. The purified enzyme from the propositus contained two components, a minor fraction (about 2–5%) which behaved similarly to the normal enzyme during the purification procedure, and a major fraction (>95%) which could not be purified by the same procedure. The major fraction demonstrated a number of other properties which differed from the normal. These included a tendency to form aggregates, increased heat sensitivity and altered nucleotide substrate specificity. The smaller fraction appeared to have effectively identical properties to that of the normal enzyme. In keeping with its X‐linked mode of inheritance, phosphoglycerate kinase from all normal tissues appeared to have identical kinetic properties, although evidence for minor variations, presumably due to post‐translational modifications, was obtained.