TY - JOUR
T1 - Ornithine-δ-transaminase from the liver fluke Fasciola hepatica and the blood fluke Schistosoma mansoni
T2 - A comparative study
AU - Goldberg, M.
AU - Flescher, E.
AU - Gold, D.
AU - Lengy, J.
PY - 1980
Y1 - 1980
N2 - 1. 1. The biochemical properties of ornithine-δ-transaminase (OTA) from Schistosoma mansoni and Fasciola hepatica were compared. 2. 2. The OTA from both flukes could be solubilized to different degrees by various detergent mixtures. 3. 3. The pH optimum for the enzymatic activity was 8-8.5. 4. 4. The Km values of OTA from F. hepatica were 3.29 and 1.81 mM for ornithine and α-ketoglutarate, respectively, and of OTA from S. mansoni-1.53 and 2.07 mM. 5. 5. The enzyme showed the highest affinity for α-ketoglutarate from among seven keto acids evaluated. 6. 6. OTA was inhibited by known pyridoxal phosphate inhibitors as well as by several structural analogues of its two substrates.
AB - 1. 1. The biochemical properties of ornithine-δ-transaminase (OTA) from Schistosoma mansoni and Fasciola hepatica were compared. 2. 2. The OTA from both flukes could be solubilized to different degrees by various detergent mixtures. 3. 3. The pH optimum for the enzymatic activity was 8-8.5. 4. 4. The Km values of OTA from F. hepatica were 3.29 and 1.81 mM for ornithine and α-ketoglutarate, respectively, and of OTA from S. mansoni-1.53 and 2.07 mM. 5. 5. The enzyme showed the highest affinity for α-ketoglutarate from among seven keto acids evaluated. 6. 6. OTA was inhibited by known pyridoxal phosphate inhibitors as well as by several structural analogues of its two substrates.
UR - http://www.scopus.com/inward/record.url?scp=49149143862&partnerID=8YFLogxK
U2 - 10.1016/0305-0491(80)90168-6
DO - 10.1016/0305-0491(80)90168-6
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AN - SCOPUS:49149143862
SN - 0305-0491
VL - 65
SP - 605
EP - 613
JO - Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
IS - 4
ER -