[Chaperone-like activity of beta-casein and thermal stability of alcohol dehydrogenase].
To elucidate the correlation of structural peculiarities of beta-casein and their chaperon-like activity the modified forms of the protein (with cysteinyl residues introduced in polypeptide chain) were investigated. The aggregation of native and recombinant beta-caseins was studied as well as their chaperon-like activity towards alcohol dehydrogenase thermal aggregation. It was shown that physico-chemical and chaperone-like properties ofdimeric and oligomeric forms ofbeta-casein (which formation is due to intermolecular disulfide bonds) differ significantly from monomeric forms. It was found that thermal stability of alcohol dehydrogenase depends on beta-casein concentration.
N L
NL
Zakharchenko
T A
TA
Konnova
N E
NE
Gogoleva
D A
DA
Faĭzullin
T
T
Haertle
Iu F
IuF
Zuev
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D000818:Animals; D002364:Caseins / Q000737:chemistry*; D002417:Cattle; D006736:Horses; D006358:Hot Temperature; D018832:Molecular Chaperones / Q000737:chemistry*; D055550:Protein Stability
D002364:Caseins; D018832:Molecular Chaperones; D000426:Alcohol Dehydrogenase