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Journal Abstract Search
147 related items for PubMed ID: 7410385
1. Stereospecificity of sodium borohydride reduction of Schiff bases at the active site of aspartate aminotransferase. Zito SW, Martinez-Carrion M. J Biol Chem; 1980 Sep 25; 255(18):8645-9. PubMed ID: 7410385 [Abstract] [Full Text] [Related]
3. Stereospecificity of sodium borohydride reduction of tyrosine decarboxylase from Streptococcus faecalis. Vederas JC, Reingold ID, Sellers HW. J Biol Chem; 1979 Jun 25; 254(12):5053-7. PubMed ID: 36380 [Abstract] [Full Text] [Related]
4. Stereochemistry of sodium borohydride reduction of tryptophan synthase of Escherichia coli and its amino acid Schiff's bases. Miles EW, Houck DR, Floss HG. J Biol Chem; 1982 Dec 10; 257(23):14203-10. PubMed ID: 6754725 [Abstract] [Full Text] [Related]
5. Differential scanning calorimetry of cytoplasmic aspartate transaminase. Relimpio A, Iriarte A, Chlebowski JF, Martinez-Carrion M. J Biol Chem; 1981 May 10; 256(9):4478-88. PubMed ID: 7217092 [Abstract] [Full Text] [Related]
6. Site-specific methylation of a strategic lysyl residue in aspartate aminotransferase. Roberts WJ, Hubert E, Iriarte A, Martinez-Carrion M. J Biol Chem; 1988 May 25; 263(15):7196-202. PubMed ID: 3130380 [Abstract] [Full Text] [Related]
7. Stereochemistry of holoaspartate transaminase after modification of the active site Lys-258. Martinez-Carrion M, Slebe JC, Gonzalez M. J Biol Chem; 1979 May 10; 254(9):3160-2. PubMed ID: 429338 [Abstract] [Full Text] [Related]
8. The ionization states of the 5'-phosphate group in the various coenzyme forms bound to mitochondrial aspartate aminotransferase. Sanchez-Ruiz JM, Iriarte A, Martinez-Carrion M. Arch Biochem Biophys; 1991 Apr 10; 286(1):38-45. PubMed ID: 1897957 [Abstract] [Full Text] [Related]
9. Reversible modification of amino groups in aspartate aminotransferase. Gilbert HF, O'Leary MH. Biochim Biophys Acta; 1977 Jul 08; 483(1):79-89. PubMed ID: 18199 [Abstract] [Full Text] [Related]
10. A simple method for determination of stereospecificity of aminotransferases for C-4' hydrogen transfer of the coenzyme. Nishimura K, Ito J, Yoshimura T, Esaki N, Soda K. Bioorg Med Chem; 1994 Jul 08; 2(7):605-7. PubMed ID: 7858965 [Abstract] [Full Text] [Related]
11. Reaction of pyridoxal 5'-sulfate with apoenzyme of aspartate aminotransferase. Covalent labeling of the protein with elimination of sulfate. Yang IY, Khomutov RM, Metzler DE. Biochemistry; 1974 Sep 10; 13(19):3877-84. PubMed ID: 4472277 [No Abstract] [Full Text] [Related]
12. Stereospecific labilization of the C-4' pro-S hydrogen of pyridoxamine 5'-phosphate in aspartate aminotransferase. Activators and inhibitors. Tobler HP, Gehring H, Christen P. J Biol Chem; 1987 Jul 05; 262(19):8985-9. PubMed ID: 2885326 [Abstract] [Full Text] [Related]
13. Inorganic phosphate binding and electrostatic effects in the active center of aspartate aminotransferase apoenzyme. Martinez-Liarte JH, Iriarte A, Martinez-Carrion M. Biochemistry; 1992 Mar 17; 31(10):2712-9. PubMed ID: 1547211 [Abstract] [Full Text] [Related]
14. Carbamylation of aspartate transaminase and the pK value of the active site lysyl residue. Slebe JC, Martinez-Carrion M. J Biol Chem; 1976 Sep 25; 251(18):5663-9. PubMed ID: 965383 [Abstract] [Full Text] [Related]
15. The active site of Sulfolobus solfataricus aspartate aminotransferase. Birolo L, Arnone MI, Cubellis MV, Andreotti G, Nitti G, Marino G, Sannia G. Biochim Biophys Acta; 1991 Nov 15; 1080(3):198-204. PubMed ID: 1954227 [Abstract] [Full Text] [Related]
16. Aspartate aminotransferase: reaction of apoenzyme with 3-substituted coenzyme analogs. Mora S, Bocharov AL, Ivanov VI, Kapeiskii MY, Mamaeva OK, Stambolieva NA. Mol Biol; 1972 Nov 15; 6(1):96-102. PubMed ID: 5086745 [No Abstract] [Full Text] [Related]
17. Porcine cytosolic aspartate aminotransferase reconstituted with [4'-13C]pyridoxal phosphate. pH- and ligand-induced changes of the coenzyme observed by 13C NMR spectroscopy. Higaki T, Tanase S, Nagashima F, Morino Y, Scott AI, Williams HJ, Stolowich NJ. Biochemistry; 1991 Mar 05; 30(9):2519-26. PubMed ID: 2001379 [Abstract] [Full Text] [Related]