Malate dehydrogenase (MDH), a commo

Malate dehydrogenase (MDH), a common enzyme in the tricarboxylic acid cycle,
is composed of two identical subunits that are held together by varying interactions [4].
These two subunits can dissociate without losing catalytic activity and reassemble in the
presence of substrate. Each subunit has a molecular weight about 35000 daltons and
contains one binding site for a c()~p.zyme. Malate dehydrogenase activity is measured with
spectrophotometer that monitors absorbance at 340 nm due to NAD reduction or NADH
oxidation. With oxaloacetate and NADH as substrates, initial reaction velocities are about
four times greater than that with malate and NAD as substrates (Table 2) [9, 10].

Kết quả (Anh) 1:

Malate dehydrogenase (MDH), a common enzyme in the tricarboxylic acid cycle,is composed of two identical subunits that are held together by varying interactions [4].These two subunits can dissociate without losing catalytic activity and reassemble in thepresence of substrate. Each subunit has a molecular weight about 35000 daltons andcontains one binding site for a c () ~ p. zyme. Malate dehydrogenase activity is measured withspectrophotometer absorbance at 340 nm that monitors due to NAD reduction or NADHoxidation. With oxaloacetate and NADH as substrates, the initial reaction velocities are aboutfour times greater than that with malate and NAD as substrates (Table 2) [9, 10].

Kết quả (Anh) 2:

Malate dehydrogenase (MDH), a common enzyme in the tricarboxylic acid cycle,
is composed of two identical subunits together by varying giữ được interactions [4].
These two subunits can dissociate and reassemble without Losing catalytic activity in the
presence of substrate. Each subunit has a molecular weight about 35000 Daltons and
contains one binding site for ac () ~ p.zyme. Malate dehydrogenase activity is measured with
spectrophotometer absorbance at 340 nm monitors có Due NADH to NAD reduction or
oxidation. With oxaloacetate and NADH as substrates, initial reaction velocities are about
four times greater than with malate and NAD có as substrates (Table 2) [9, 10].