A novel glutamate dehydrogenase from bovine brain: purification and characterization.
A soluble form of novel glutamate dehydrogenase has been purified from bovine brain. The preparation was homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and composed of six identical subunits having a subunit size of 57,500 Da. The biochemical properties of glutamate dehydrogenase such as N-terminal amino acids sequences, kinetic parameters, amino acids analysis, and optimum pH were examined in both reductive amination of alpha-ketoglutarate and oxidative deamination of glutamate. N-terminal amino acid sequences of the bovine brain enzyme showed the significant differences in the first 5 amino acids compared to other glutamate dehydrogenases from various sources. These results indicate that glutamate dehydrogenase isolated from bovine brain is a novel polypeptide.
Lee
J
J
Department of Biochemistry, College of Medicine, University of Ulsan, Seoul, Korea.
Kim
S W
SW
Cho
S W
SW
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D003067:Coenzymes / Q000378:metabolism; D005969:Glutamate Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D018698:Glutamic Acid; D006863:Hydrogen-Ion Concentration; D007656:Ketoglutaric Acids / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010084:Oxidation-Reduction; D017421:Sequence Analysis; D012995:Solubility; D013379:Substrate Specificity
D000596:Amino Acids; D003067:Coenzymes; D007656:Ketoglutaric Acids; D018698:Glutamic Acid; D005969:Glutamate Dehydrogenase