Pahlich E
Planta. 2014; 110(3):267-78.
PMID: 24474403
DOI: 10.1007/BF00387638.
Hill M, Carroll E, Vang M, Addington T, Toney M, Larsen D
J Am Chem Soc. 2010; 132(47):16953-61.
PMID: 21058708
PMC: 3021986.
DOI: 10.1021/ja107054x.
McCurdy H, CANTINO E
Plant Physiol. 1960; 35(4):463-76.
PMID: 16655373
PMC: 405989.
DOI: 10.1104/pp.35.4.463.
Evangelopoulos A, SIZER I
Proc Natl Acad Sci U S A. 1963; 49(5):638-43.
PMID: 16591081
PMC: 299942.
DOI: 10.1073/pnas.49.5.638.
Hughes R, JENKINS W, FISCHER E
Proc Natl Acad Sci U S A. 1962; 48:1615-8.
PMID: 14449825
PMC: 221009.
DOI: 10.1073/pnas.48.9.1615.
INTERACTION OF ASPARTATE AMINOTRANSFERASE WITH AMINO ACIDS.
Scotto P, SCARDI V
Biochem J. 1965; 95:657-60.
PMID: 14342499
PMC: 1206790.
DOI: 10.1042/bj0950657.
[IMMUNOLOGY AND ENZYME KINETICS OF GLUTAMATE-OXALACETATE-TRANSAMINASE (GOT) AND GLUTAMATE-PYRUVATE-TRANSAMINASE (GPT). I. CURRENT RESULTS AND PROBLEMS. METHODOLOGY. STUDIES ON KINETICS OF THE INHIBITING ACTION OF TRANSAMINASE ANTIBODIES].
Massarrat S, Lang N
Klin Wochenschr. 1965; 43:510-4.
PMID: 14304914
DOI: 10.1007/BF01486092.
PROPERTIES OF CRYSTALLINE L-ASPARTATE 4-CARBOXY-LYASE FROM ACHROMOBACTER SP.
Wilson E, Kornberg H
Biochem J. 1963; 88:578-87.
PMID: 14071532
PMC: 1202217.
DOI: 10.1042/bj0880578.
The N-terminal groups of glutamic aspartic transaminase.
TURANO C, VECCHINI P, Giartosio A
Experientia. 1962; 18:544-5.
PMID: 13994801
DOI: 10.1007/BF02172165.
[Methods and value of determination of glutamic acid dehydrogenase activity in the serum. A contribution to the importance of examination of enzyme relations in the serum].
Schmidt E, Schmidt F
Klin Wochenschr. 1962; 40:962-9.
PMID: 13991973
DOI: 10.1007/BF01481421.
The binding of pyridoxal 5-phosphate to aspartate aminotransferase of pig heart.
SCARDI V, Scotto P, Iaccarino M, Scarano E
Biochem J. 1963; 88:172-5.
PMID: 13976516
PMC: 1203869.
DOI: 10.1042/bj0880172.
Determination of half-reaction equilibrium in a ping-pong enzyme mechanism.
Smith G, Harrison R, Eisenthal R
Neurochem Res. 1996; 21(9):1061-4.
PMID: 8897469
DOI: 10.1007/BF02532416.
Effect of temperature on the spectral properties of glutamic-aspartic transaminase and pyridoxal phosphate.
Evangelopoulus A
Experientia. 1967; 23(9):708-9.
PMID: 6062878
DOI: 10.1007/BF02154125.
Acylation of aspartate aminotransferase.
TURANO C, Giartosio A, Riva F, BARONCELLI V
Biochem J. 1967; 104(3):970-7.
PMID: 6049935
PMC: 1271239.
DOI: 10.1042/bj1040970.
Amino acid composition and terminal residues of aspartate aminotransferase from ox heart.
Marino G, SCARDI V, Zito R
Biochem J. 1966; 99(3):595-8.
PMID: 6007357
PMC: 1265046.
DOI: 10.1042/bj0990595.
Purification and general properties of aspartate aminotransferase of ox heart.
Marino G, Greco A, SCARDI V, Zito R
Biochem J. 1966; 99(3):589-94.
PMID: 6007356
PMC: 1265045.
DOI: 10.1042/bj0990589.
Binding sites in the active center of glutamic-aspartic transaminase.
Evangelopoulos A, SIZER I
Experientia. 1965; 21(10):576.
PMID: 5868486
DOI: 10.1007/BF02151539.
Aminotransferases of Agrobacterium tumefaciens. Transamination between tryptophan and phenylpyruvate.
Sukanya N, Vaidyanathan C
Biochem J. 1964; 92(3):594-8.
PMID: 5837443
PMC: 1206107.
DOI: 10.1042/bj0920594.
Dissociation of the prosthetic group of aspartate aminotransferase.
Dixon H, Severin E
Biochem J. 1968; 110(2):18P-19P.
PMID: 5726192
PMC: 1187245.
DOI: 10.1042/bj1100018p.
The influence of chloride and other univalent inorganic anions on the visible-absorption spectrum of aspartate aminotransferase.
Bergami M, Marino G, SCARDI V
Biochem J. 1968; 110(3):471-3.
PMID: 5701677
PMC: 1187374.
DOI: 10.1042/bj1100471.