[Isolation and physico-chemical properties of a protein, included in an endotoxin from Yersinia pseudotuberculosis].
A major protein of the endotoxin from Yersinia pseudotuberculosis was isolated from the complex lipid A--protein by treatment with SDS and triton X-100 followed by gel-chromatography on Sephacryl S-300. Protein has apparent molecular mass 40 kDa and alanine as N-terminal amino acid residue. CD and IR spectroscopy conformational changes of the protein molecule in the process of its isolation. The thermal and pH stabilities of the protein were investigated by the methods of intrinsic fluorescence and differential scanning microcalorimetry. The isolated protein revealed two thermal transitions (at 30-35 and 50-55 degrees C), which depend on Ca2+ concentration.
L I
LI
Fedoreeva
T F
TF
Solov'eva
Iu S
IuS
Ovodov
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002118:Calcium / Q000494:pharmacology; D002152:Calorimetry, Differential Scanning; D002850:Chromatography, Gel; D002942:Circular Dichroism; D004731:Endotoxins / Q000302:isolation & purification*; D005453:Fluorescence; D006863:Hydrogen-Ion Concentration; D013055:Spectrophotometry, Infrared; D013205:Staphylococcal Protein A; D015011:Yersinia pseudotuberculosis
D000596:Amino Acids; D001426:Bacterial Proteins; D004731:Endotoxins; D013205:Staphylococcal Protein A; D002118:Calcium
Vydelenie i fiziko-khimicheskaia kharakteristika belka, vkhodiashchego v sostav éndotaksina iz Yersinia pseudotuberculosis.