Functional role of arginine residues in glutamic acid decarboxylase from brain and bacteria
暂无分享，去创建一个
[1] J F Riordan,et al. Arginyl residues: anion recognition sites in enzymes. , 1977, Science.
[2] V. Armstrong,et al. Modification of an essential arginine in Escherichia coli DNA‐dependent RNA polymerase , 1976, FEBS letters.
[3] S. Schuster,et al. Essential arginyl residues in mitochondrial adenosine triphosphatase. , 1976, The Journal of biological chemistry.
[4] H. Gilbert,et al. Arginine as a substrate binding site in aspartate aminotransferase. , 1975, Biochemical and biophysical research communications.
[5] R. Scandurra,et al. Essential arginyl residues in aspartate aminotransferases. , 1975, Biochemical and biophysical research communications.
[6] J. Wu,et al. PROPERTIES OF BRAIN l‐GLUTAMATE DECARBOXYLASE: INHIBITION STUDIES 1 , 1974, Journal of neurochemistry.
[7] J. Wu,et al. Purification and characterization of glutamate decarboxylase from mouse brain. , 1973, The Journal of biological chemistry.
[8] M. Fonda. Glutamate decarboxylase. Substrate specificity and inhibition by carboxylic acids. , 1972, Biochemistry.
[9] E. Roberts,et al. Some properties of L-glutamic decarboxylase in mouse brain. , 1963, Biochemical pharmacology.
[10] G. Tunnicliff,et al. Mechanism of inactivation of brain glutamic decarboxylase by 3-bromopyruvate. , 1978, The International journal of biochemistry.