β-Alanine suppresses heat inactivation of lactate dehydrogenase

Abstract

β-Alanine exhibits neurotransmitter activity and is a component of the anti-glycation agent carnosine. We propose that β-alanine may have additional properties which may be of physiological significance. Interestingly, stress modulates the level of β-alanine, which regulates excitotoxicity responses and prevents neuronal cell death. We hypothesize that β-alanine's protective role may involve preservation of enzyme structure and function, suggesting that β-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 β-alanine. We observed that β-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 β-alanine has chaperone-like activity and may play a cellular role in the preservation of enzyme function.

Keywords: :

• β-Alanine
• lactate dehydrogenase
• chaperone
• denaturation