REVERSIBLE AND IRREVERSIBLE MODIFICATIONS OF BETA-LACTOGLOBULIN UPON EXPOSURE TO HEAT
被引:122
作者:
CAIROLI, S
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机构:
UNIV MILAN,CTR INTERUNIV STUDIO MACROMOLEC INFORMAZ,I-20133 MILAN,ITALYUNIV MILAN,CTR INTERUNIV STUDIO MACROMOLEC INFORMAZ,I-20133 MILAN,ITALY
CAIROLI, S
[1
]
IAMETTI, S
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h-index: 0
机构:
UNIV MILAN,CTR INTERUNIV STUDIO MACROMOLEC INFORMAZ,I-20133 MILAN,ITALYUNIV MILAN,CTR INTERUNIV STUDIO MACROMOLEC INFORMAZ,I-20133 MILAN,ITALY
IAMETTI, S
[1
]
BONOMI, F
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h-index: 0
机构:
UNIV MILAN,CTR INTERUNIV STUDIO MACROMOLEC INFORMAZ,I-20133 MILAN,ITALYUNIV MILAN,CTR INTERUNIV STUDIO MACROMOLEC INFORMAZ,I-20133 MILAN,ITALY
BONOMI, F
[1
]
机构:
[1] UNIV MILAN,CTR INTERUNIV STUDIO MACROMOLEC INFORMAZ,I-20133 MILAN,ITALY
来源:
JOURNAL OF PROTEIN CHEMISTRY
|
1994年
/
13卷
/
03期
关键词:
HEAT PROTEIN DENATURATION;
PROTEIN SURFACE HYDROPHOBICITY;
PROTEIN AGGREGATION;
BETA-LACTOGLOBULIN;
D O I:
10.1007/BF01901568
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Modifications in the exposure to the solvent of hydrophobic residues, changes in their organization into surface hydrophobic patches, and alterations in the dimerization equilibrium of beta-lactoglobulin upon thermal treatment at neutral pH were studied. Exposure of tryptophan residues was temperature dependent and was essentially completed on the time scale of seconds. Reorganization of generic hydrophobic protein patches on the protein surface was monitored through binding of 1,8-anilinonaphthalenesulfonate, and was much slower than changes in tryptophan exposure. Different phases in surface hydrophobicity changes were related to the swelling and the subsequent collapse of the protein, which formed a metastable swollen intermediate. Heat treatment of beta-lactoglobulin also resulted in the formation of soluble oligomeric aggregates. The aggregation process was studied as a function of temperature, demonstrating that (i) dimer dissociation was a necessary step in a sequential polymerization mechanism and (ii) cohesion of hydrophobic patches was the major driving force for aggregation.