Molecular analysis of genetic mutation in electrophoretic variant of human lactate dehydrogenase-A(M) subunit.
An electrophoretic variant of lactate dehydrogenase-A (M) subunit was discovered in a patient with multiple myeloma. DNA analysis of the variant allele revealed a nucleotide substitution (transition) of C to T at codon 314 (CGT-TGT), and this mutation resulted in the replacement of an arginine by a cysteine (R314C). This amino acid replacement affects the net charge of the subunit and makes the LDH-A variant have a faster electrophoretic mobility. The responsible missense mutation created a new restriction site, AGGCCT, which can be simply detected by endonuclease AatI digestion. In addition, four synonymous substitutions with no amino-acid replacements were found at codons 51, 119, 163 and 175 in the LDH-A gene from the patient.
Sudo
K
K
Department of Laboratory Medicine, Jikei University School of Medicine, Daisan Hospital, Komae, Japan.
Maekawa
M
M
Shioya
M
M
Ikeda
K
K
Takahashi
N
N
Isogai
Y
Y
Li
S S
SS
Kanno
T
T
Machida
K
K
Toriumi
J
J
D000368:Aged; D000595:Amino Acid Sequence; D000818:Animals; D004586:Electrophoresis; D005260:Female; D006801:Humans; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000097:blood / Q000235:genetics*; D008969:Molecular Sequence Data; D009101:Multiple Myeloma / Q000201:enzymology; D009154:Mutation; D016133:Polymerase Chain Reaction; D012689:Sequence Homology, Nucleic Acid
D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase