Conformational Drift of Lactate Dehydrogenase
نویسندگان
چکیده
منابع مشابه
Conformational stability of lactate dehydrogenase from Bacillus thermus-aquaticus [proceedings].
Proteins are synthesized and enzymes can function at surprisingly high temperatures in thermophilic micro-organisms. This temperature is about 90°C in the case of Bacillus thermus-aquaticus (A.T.C.C. 25104). Lactate dehydrogenase (EC 1.1.1.27) was isolated from this micro-organism, and the temperature dependence of the rate of pyruvate reduction and thermodynamic parameters of heat inactivation...
متن کاملCharacterization of rabbit lactate dehydrogenase-M and lactate dehydrogenase-H cDNAs. Control of lactate dehydrogenase expression in rabbit muscle.
Two cDNA clones were isolated, one corresponding to the mRNA coding for lactate dehydrogenase-M (LDH-M), the other to the mRNA coding for lactate dehydrogenase-H (LDH-H). The cDNA inserts consist of the entire open reading frame for LDH-M and a partial sequence, from amino acid 117 to 332, for LDH-H. Using these two clones as probes we demonstrate that: (a) the abundance of mRNA is muscle-type ...
متن کاملLACTATE DEHYDROGENASE Elevation ofserum lactate dehydrogenasecommences
Heart tissue injury may release cardiac enzymes into the circulation and elevate serum enzyme levels (LaDue, Wroblewski, and Karmen, 1954). Many enzymes become raised, but three enzymesaspartate aminotransferase (EC 2.6.1.1), creatine kinase (EC 2.7.3.2), and lactate dehydrogenase (EC 1.1.1.27)-have proved of particular diagnostic value. In addition, determination of lactate dehydrogenase isoen...
متن کاملSerum Lactate Dehydrogenase Elevation
Activity of total lactate dehydrogenase (LDH) and that of the heat-stable isozyme (LDH-1) was measured by the method of Strandjord and Clayson in the serum of 62 cardiac patients with congenital and valvular heart disease before and after cardiac catheterization and at follow-up examination after cardiac surgery. A universal elevation of both total and heat-stable LDH was found in patients with...
متن کاملPorcine Heart Lactate Dehydrogenase
The tinetics of NADH, 3-thionicotinamide adenine dinucleotide (TNAD), and oxamate binding to the H4 isoenzyme of lactate dehydrogenase from the pig has been investigated by temperature jump techniques. The dissociation rate constant for TNAD is considerably larger than for NADH, whereas the recombination rate constant is smaller for the oxidized coenzyme than for the reduced molecule. The kinet...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1986
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(86)83597-4