Structural changes and aggregation process of Cu/containing amine oxidase in the presence of 2,2,2'-trifluoroethanol.
Journal - Protein and peptide letters (Netherlands )
Conformational and structural changes of lentil seedlings amine oxidase (LSAO) were studied in the presence of trifluoroethanol (TFE) by spectroscopic and analytical techniques. At TFE concentrations up to 5%, the induction of a structural transition from beta-sheet to alpha-helix and up to 10% TFE a structural transition from alpha-helix to beta-sheet as well as inactivation of the enzyme are observed. At TFE concentrations between 10-35%, LSAO proves to be prone to aggregation and beyond 35% TFE leads to a non-native protein structure with a high alpha-helix content. The obtained results revealed that the aggregation of LSAO is strongly linked to the nature of secondary structures.
|ISSN : ||0929-8665|
|Mesh Heading : ||Amine Oxidase (Copper-Containing) Circular Dichroism Hot Temperature Protein Conformation Protein Denaturation Protein Folding Protein Structure, Secondary Trifluoroethanol isolation & purification|
|Mesh Heading Relevant : ||chemistry pharmacology|
Two-state irreversible thermal denaturation of Euphorbia characias latex amine oxidase.
Journal - Biophysical chemistry (Netherlands )
Thermal denaturation of Euphorbia latex amine oxidase (ELAO) has been studied by enzymatic activity, circular dichroism and differential scanning calorimetry. Thermal denaturation of ELAO is shown to be an irreversible process. Checking the validity of two-state it really describes satisfactorily the thermal denaturation of ELAO. Based on this model we obtain the activation energy, parameter T(*) (the absolute temperature at which the rate constant of denaturation is equal to 1 min(-1)), and total enthalpy of ELAO denaturation. HPLC experiments show that the thermal denatured enzyme conserves its dimeric state. The N(2)-->kD(2) model for thermal denaturation of ELAO is proposed: where N(2) and D(2) are the native and denatured dimer, respectively.
|ISSN : ||0301-4622|
|Mesh Heading : ||Amine Oxidase (Copper-Containing) Euphorbia Kinetics Latex Plant Proteins Thermodynamics chemistry|
|Mesh Heading Relevant : ||Protein Denaturation Temperature chemistry enzymology|