Beta-alanine suppresses heat inactivation of lactate dehydrogenase.
Beta-Alanine exhibits neurotransmitter activity and is a component of the anti-glycation agent carnosine. We propose that beta-alanine may have additional properties which may be of physiological significance. Interestingly, stress modulates the level of beta-alanine, which regulates excitotoxicity responses and prevents neuronal cell death. We hypothesize that beta-alanine's protective role may involve preservation of enzyme structure and function, suggesting that beta-alanine may act as a chemical chaperone. We used light scattering, enzyme activity and intrinsic fluorescence to monitor heat-induced changes in lactate dehydrogenase (LDH) in the presence and absence of beta-alanine. We observed that beta-alanine suppressed heat-induced LDH inactivation, prevented LDH aggregation, ameliorated the decrease in intrinsic fluorescence and reactivated thermally denatured LDH. These observations support the hypothesis that beta-alanine has chaperone-like activity and may play a cellular role in the preservation of enzyme function.
Mehta
Ankur D
AD
Department of Biochemistry, Kansas City University of Medicine and Biosciences, 1750 Independence Avenue, Kansas City, MO 64106-1453, USA.
Seidler
Norbert W
NW
D001671:Biochemistry / Q000379:methods; D006358:Hot Temperature; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D008027:Light; D008291:Malate Dehydrogenase / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D011489:Protein Denaturation; D017510:Protein Folding; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013997:Time Factors; D015091:beta-Alanine / Q000737:chemistry / Q000494:pharmacology*
D018832:Molecular Chaperones; D015091:beta-Alanine; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase