title: Prevention of thermal inactivation and aggregation of lysozyme by polyamines.
abstract: Proteins tend to form inactive aggregates at high temperatures. We show that polyamines, which have a relatively simple structure as oligoamids, effectively prevent thermal inactivation and aggregation of hen egg lysozyme. In the presence of additives, including arginine and guanidine (100 microM), more than 30% of 0.2 mg x mL(-1) lysozyme in sodium phosphate buffer (pH 6.5) formed insoluble aggregates by heat treatment (98 degrees C for 30 min). However, in the presence of 50 mm spermine or spermidine, no aggregates were observed after the same heat treatment. The residual activity of lysozyme after this heat treatment was very low (< 5%), even in the presence of 100 microM arginine and guanidine, while it was maintained at approximately 50% in the presence of 100 microM spermine and spermidine. These results imply that polyamines are new candidates as molecular additives for preventing the thermal aggregation and inactivation of heat-labile proteins.
authors: School of Materials Science, Japan Advanced Institute of Science and Technology, Ishikawa, Japan.
authors: Motonori
authors: M
authors: Kudou
authors: Kentaro
authors: K
authors: Shiraki
authors: Shinsuke
authors: S
authors: Fujiwara
authors: Tadayuki
authors: T
authors: Imanaka
authors: Masahiro
authors: M
authors: Takagi
mesh_terms: D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D004795:Enzyme Stability / Q000187:drug effects; D009113:Muramidase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D009994:Osmolar Concentration; D011073:Polyamines / Q000494:pharmacology*; D011489:Protein Denaturation / Q000187:drug effects; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors
chemical_list: D011073:Polyamines; D009113:Muramidase