Studies on Pyruvate Kinase (PK) Deficiency

Imamura, Kiichi; Tanaka, Takehiko; Nishina, Toshihiro; Nakashima, Kenichiro; Shiro, Motoo

doi:10.1093/oxfordjournals.jbchem.a130344

Cited by 94 publications

(10 citation statements)

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“…Type R is closely similar to type L in immunological properties [2], genetic properties [9], and amino acid composition [4]. However, various models have been proposed to explain its anomalous electrophoretic mobility [9,10], although there is no general agreement on this problem, For conflation of the structural differences of these isozymes, their primary st~ctures must be compared, The present work demonstrates the similarities and the dissimilarities in the peptide maps obtained by limited proteolytic digestion of the four pyruvate kinase isozymes.…”

Section: In~du~tionmentioning

confidence: 89%

Peptide mapping by limited proteolysis of four pyruvate kinase isozymes

Saheki

Tanaka

1978

FEBS Letters

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Section: In~du~tionmentioning

confidence: 89%

Peptide mapping by limited proteolysis of four pyruvate kinase isozymes

Saheki

Tanaka

1978

FEBS Letters

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“…It has been previously demonstrated that these enzymes are kinetically [ 1,2] and immunologltally [3-51 related. In some cases liver (Ltype) pyruvate kinase from patients with hereditary erythrocyte pyruvate kinase deficiency was shown to be defective [2,. Erythrocyte and L-type enzymes, however, can be distinguished by their electrophoretic mobilities [2,9] .…”

Section: Introductionmentioning

confidence: 99%

“…In some cases liver (Ltype) pyruvate kinase from patients with hereditary erythrocyte pyruvate kinase deficiency was shown to be defective [2,. Erythrocyte and L-type enzymes, however, can be distinguished by their electrophoretic mobilities [2,9] . Some authors [9] have suggested that erythrocyte enzyme might be a hybrid between Ltype and non-L-type subunits: the demonstration by Peterson et al [lo] that, by sodium dodecylsulphate-acrylamlde gel electrophoresis, erythrocyte pyruvate kinase was resolved into two distinct bands with similar mobility, supported this assumption.…”

Section: Introductionmentioning

confidence: 99%

Evidence for a postsynthetic proteolytic transformation of human erythrocyte pyruvate kinase into L‐type enzyme

1977

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“…This variant enzyme was characterized by increased K0.5S (phosphoenolpyruvate), thermal instability, and slow electrophoretic mobility (13). Because the slow electrophoretic mobility of this variant PK had been demonstrated in both erythrocytes and liver (14), a structural mutation within the region common to both L-and R-type PKs was expected. Because of the consanguineous marriage of the parents, who were second cousins, the patients were thought to be homozygous for the mutant PK gene.…”

mentioning

confidence: 99%

cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia.

Kanno¹,

Fujii²,

Hirono³

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACTcDNA clones for human R-type pyruvate kinase (PK) were isolated from a human reticulocyte cDNA library, constructed by PCR with a single gene-spedflc primer. The full-length cDNA was 2060 base pairs long, and the cDNA encoded 574 amino adds, the same number as that by rat R-type PK. Compared with human L-type PK, R-type PK was 31 amino acids longer at the amino terminus. We also cloned and characterized R-type PK cDNA clones from patients with hereditary hemolytic anemia from a PK deficiency, PK Tokyo. A single nucleotide substitution (ACG to ATG) was found at nucleotide 1151 of the coding sequence of the R-type PK, which caused an amino acid substitution, Thr3N -Met. Dot blot hybridization of PCR-ampifled genomic DNA from patients and their parents by allele-specific oligonucleotide probes showed that the patients were homozygous for this nucleotide change and that the parents, who were second cousins, were heterozygous. To confirm that the nucleotide change was responsible for the variant phenotype, we expressed the L-type PK with the single amino acid change in Escherichia coil and characterized the enzyme. The variant PK was thermolabile and moved slowly in the polyacrylamide gel buffered in 10 mM Tris-HCI, pH 8.3; these characteristics were fully compatible with data obtained from the patient's PK. From these results, we concluded that enzymatic stability of the variant was affected by the point mutation of the PK-encoding gene.

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Studies on Pyruvate Kinase (PK) Deficiency

Cited by 94 publications

References 0 publications

Peptide mapping by limited proteolysis of four pyruvate kinase isozymes

Peptide mapping by limited proteolysis of four pyruvate kinase isozymes

Evidence for a postsynthetic proteolytic transformation of human erythrocyte pyruvate kinase into L‐type enzyme

cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia.

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