Role of amyloid type cross β-structure in the formation of soluble aggregate and gel in heat-induced ovalbumin

Journal of Agricultural and Food Chemistry

Volumn 53, Issue 4, 2005, Pages 1254-1257

  Azakami, H ^a   Mukai, A ^a   Kato, A ^a  

^a YAMAGUCHI UNIVERSITY   (Japan)

Author keywords

Amyloid fibril formation; Heat induced gel; Ovalbumin; Soluble heat denatured aggregate; Thioflavin T

Indexed keywords

AMYLOID; LYSOZYME; OVALBUMIN; OVOTRANSFERRIN; THIOFLAVINE;

ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONTROLLED STUDY; CORRELATION ANALYSIS; FLUORESCENCE; GEL; HEAT TREATMENT; NONHUMAN; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE;

AMYLOID; FLUORESCENT DYES; GELS; HEAT; HYDROGEN-ION CONCENTRATION; OVALBUMIN; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; THIAZOLES;

EID: 13944261144     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf049325f     Document Type: Article

References (13)

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