Biomaterial Database

Free radical inactivation of lactate dehydrogenase. 1976

J D Buchanan, and D A Armstrong

The enzyme lactate dehydrogenase (LDH) has been irradiated under various conditions to assess the relative contributions of -H, -OH, H2O2 and -O2- to LDH inactivation, and it is concluded that -OH is the only important inactivating species. Further the effect of the selective free radicals, -(SCN)2-, -Br2- and -I2- on the activity has been studied. In neutral solution, the order of inactivating effectiveness is -I2- greater than -OH greater than -Br2- greater than -(SCN)2-. At pH 8-6, -OH and -Br2- are approximately equal in effectiveness, whereas -(SCN)2- is the least efficient. The radiation inactivation of LDH is accompanied by a loss of sulphydryl groups, and it is suggested that the primary target for radiation damage in LDH is the active site cysteine-165. Subsequent conformational changes are suggested to account for the apparent loss of coenzyme-binding ability and changes in the enzyme's kinetic parameters. The effect of bound coenzyme (NAD) on radiation-induced inactivation of N2O and air-saturated solutions was also investigated, and it is shown that NAD binding protects LDH.

UI	MeSH Term	Description	Entries
D007770	L-Lactate Dehydrogenase	A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.	Lactate Dehydrogenase,Dehydrogenase, L-Lactate,Dehydrogenase, Lactate,L Lactate Dehydrogenase
D009243	NAD	A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)	Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D003037	Cobalt Radioisotopes	Unstable isotopes of cobalt that decay or disintegrate emitting radiation. Co atoms with atomic weights of 54-64, except 59, are radioactive cobalt isotopes.	Radioisotopes, Cobalt
D005609	Free Radicals	Highly reactive molecules with an unsatisfied electron valence pair. Free radicals are produced in both normal and pathological processes. Free radicals include reactive oxygen and nitrogen species (RONS). They are proven or suspected agents of tissue damage in a wide variety of circumstances including radiation, damage from environment chemicals, and aging. Natural and pharmacological prevention of free radical damage is being actively investigated.	Free Radical
D005720	Gamma Rays	Penetrating, high-energy electromagnetic radiation emitted from atomic nuclei during NUCLEAR DECAY. The range of wavelengths of emitted radiation is between 0.1 - 100 pm which overlaps the shorter, more energetic hard X-RAYS wavelengths. The distinction between gamma rays and X-rays is based on their radiation source.	Gamma Wave,Gamma Radiation,Nuclear X-Rays,Radiation, Gamma,X-Rays, Nuclear,Gamma Radiations,Gamma Ray,Gamma Waves,Nuclear X Rays,Nuclear X-Ray,Ray, Gamma,Wave, Gamma,Waves, Gamma,X Rays, Nuclear,X-Ray, Nuclear
D013997	Time Factors	Elements of limited time intervals, contributing to particular results or situations.	Time Series,Factor, Time,Time Factor