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Items: 1 to 20 of 216

1.

Steady-state kinetics of horse-liver alcohol dehydrogenase with a covalently bound coenzyme analogue.

Kovár J, Simek K, Kucera I, Matyska L.

Eur J Biochem. 1984 Mar 15;139(3):585-91.

6.

Catalytic significance of binary enzyme-aldehyde complexes in the liver alcohol dehydrogenase reaction.

Andersson P, Kvassman J, Oldén B, Pettersson G.

Eur J Biochem. 1984 Mar 15;139(3):519-27.

7.
8.
9.

The binding of sulfonamides to horse liver alcohol dehydrogenase.

Western A, Syvertsen C, McKinley-McKee JS.

Biochem Pharmacol. 1984 Mar 1;33(5):731-8.

PMID:
6370261
10.
11.

Kinetics of native and modified liver alcohol dehydrogenase with coenzyme analogues: isomerization of enzyme-nicotinamide adenine dinucleotide complex.

Plapp BV, Sogin DC, Dworschack RT, Bohlken DP, Woenckhaus C, Jeck R.

Biochemistry. 1986 Sep 23;25(19):5396-402.

PMID:
3778867
12.

Kinetic equivalence of the active sites of alcohol dehydrogenase from horse liver.

Hadorn M, John VA, Meier FK, Dutler H.

Eur J Biochem. 1975 May;54(1):65-73.

14.

Transient kinetic studies of substrate inhibition in the horse liver alcohol dehydrogenase reaction.

Kamlay MT, Shore JD.

Arch Biochem Biophys. 1983 Apr 1;222(1):59-66.

PMID:
6340613
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