PMID- 17852555
OWN - NLM
STAT- MEDLINE
DCOM- 20080619
LR  - 20131121
IS  - 0955-3002 (Print)
IS  - 0955-3002 (Linking)
VI  - 84
IP  - 1
DP  - 2008 Jan
TI  - Inactivation of chosen dehydrogenases by the products of water radiolysis and 
      secondary albumin and haemoglobin radicals.
PG  - 15-22
AB  - PURPOSE: Inactivation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), 
      alcohol dehydrogenase (ADH) and lactate dehydrogenase (LDH) by products of water 
      radiolysis and by secondary radicals localized on haemoglobin (Hb) and human 
      albumin (HSA) was studied. MATERIALS AND METHODS: Aqueous solutions of ADH, GAPDH 
      and LDH were irradiated under air and under nitrous oxide (N2O) in the absence 
      and in the presence of Hb or HSA. In order to determine the effectiveness of 
      inactivation of the enzymes by radicals localized on Hb and HSA, the inactivation 
      efficiency determined experimentally was compared with that calculated under 
      assumption that only hydroxyl radicals are responsible for the enzyme 
      inactivation. RESULTS: In the absence of other proteins, under air, GAPDH showed 
      the highest radiation sensitivity, followed by ADH and LDH. The sequence was 
      reverse under anaerobic atmosphere. Oxygen increased considerably the 
      inactivation of GAPDH and ADH. Secondary albumin and haemoglobin radicals brought 
      about considerable inactivation of GAPGH and ADH. Albumin radicals (HSA) 
      generated under N2O inactivated GAPDH and ADH more effectively than haemoglobin 
      radicals (Hb). Under air, however, inactivation of GAPDH and ADH by haemoglobin 
      peroxyl radicals was higher than by albumin peroxyl radicals. LDH was resistant 
      to inactivation by haemoglobin and albumin radicals, and peroxides of these 
      proteins. CONCLUSIONS: In the light of these results and literature data, the 
      observed differences in the effectiveness of inactivation of the dehydrogenases 
      studied by secondary protein radicals depend on the amino acid residues present 
      at the active site and in its close neighborhood and on the number of amino acid 
      residues available on the protein surface.
FAU - Kowalczyk, Aleksandra
AU  - Kowalczyk A
AD  - Department of Molecular Biophysics, University of Lodz, Lodz, Poland. 
      olakow@biol.uni.lodz.pl
FAU - Serafin, Eligiusz
AU  - Serafin E
FAU - Puchala, Mieczyslaw
AU  - Puchala M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Int J Radiat Biol
JT  - International journal of radiation biology
JID - 8809243
RN  - 0 (Free Radicals)
RN  - 0 (Hemoglobins)
RN  - 0 (Serum Albumin)
RN  - 059QF0KO0R (Water)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.1.1.1 (Alcohol Dehydrogenase)
RN  - EC 1.1.1.27 (L-Lactate Dehydrogenase)
RN  - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
RN  - K50XQU1029 (Nitrous Oxide)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Alcohol Dehydrogenase/chemistry/radiation effects
MH  - Free Radicals/chemistry/radiation effects
MH  - Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry/radiation effects
MH  - Hemoglobins/*radiation effects
MH  - Humans
MH  - L-Lactate Dehydrogenase/chemistry/radiation effects
MH  - Nitrous Oxide/chemistry
MH  - Oxidoreductases/chemistry/*radiation effects
MH  - Oxygen/chemistry
MH  - Serum Albumin/chemistry/*radiation effects
MH  - Water/*chemistry
EDAT- 2007/09/14 09:00
MHDA- 2008/06/20 09:00
CRDT- 2007/09/14 09:00
PHST- 2007/09/14 09:00 [pubmed]
PHST- 2008/06/20 09:00 [medline]
PHST- 2007/09/14 09:00 [entrez]
AID - 781870565 [pii]
AID - 10.1080/09553000701616056 [doi]
PST - ppublish
SO  - Int J Radiat Biol. 2008 Jan;84(1):15-22. doi: 10.1080/09553000701616056.