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1 graphic analysis of allosterically inhibited L-lactate dehydrogenase.
2 n alpha-glycol-3-phosphate dehydrogenase and l-lactate dehydrogenase.
3 that these CD dimers inhibit the activity of L-lactate dehydrogenase and citrate synthase at least in
5 uce D(-)-lactate by deleting the native ldh (L-lactate dehydrogenase) and alsS (acetolactate synthase
7 tion, employing cystathionine beta-lyase and L-lactate dehydrogenase as coupling enzymes, are describ
8 tion, employing cystathionine beta-lyase and L-lactate dehydrogenase as coupling enzymes, is describe
9 3-phosphate-dehydrogenase, alpha enolase and L-lactate dehydrogenase B-chain) and in oxidative stress
11 s generated by the reduction of pyruvate via l-lactate dehydrogenase, but this enzyme does not effici
13 overexpression of a Lactobacillus helveticus L-lactate dehydrogenase in M. buryatense resulted in an
16 duced amino acid sequences of cDNAs encoding L-lactate dehydrogenase (LDH) isozymes A (muscle) and B
17 ed on reduced graphene oxide (RGO-AuNPs) and l-lactate dehydrogenase (LDH) was developed for the sens
19 bumin, 3.4 g/dL; beta2-microglobulin, 5.7 mg/L; lactate dehydrogenase (LDH), 397 IU/L; and normal liv
20 sative stress by expressing an NO.-inducible L-lactate dehydrogenase (ldh1, SACOL0222) divergently tr
21 ty in sequence and catalytic properties, the l-lactate dehydrogenases (LDHs) in lactic acid bacteria
22 mylase level, 1435 U/L (normal level, <140 U/L); lactate dehydrogenase level, 253 U/L (normal level,
24 ate kinase, phosphate acetyltransferase, and L-lactate dehydrogenase) resulted in a strain able to pr
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