The pressure-induced inactivation of mammalian enolases is accompanied by dissociation of the dimeric enzyme.

摘要: Abstract The effects of exposure to pressure on both the activity and quaternary structure rabbit brain enolases, forms αα, αγ, γγ were studied in range 1 3400 bar. Effects determined by subunit scrambling (the formation αα from αγ or vice versa). All three dimers are stable up pressures 1200 dissociation begins at bar, yielding a monomer; inactivation does not begin until is greater than 2000 Dissociation accompanied changes tryptophan fluorescence protein. However, decrease when point which starts. α monomer, other hand, unstable that produces αα. This process, also paralleled inactivation. Crosslinking enzyme with glutaraldehyde demonstrated inactive form monomeric. pressure-induced these enolase thus clearly two-step occurring. difference sensitivity due stability γ monomers required for dissociation.