The N-terminal amino acid of apolipoprotein D is putatively covalently bound to 3-hydroxy-3-methyl hexanoic acid, a key odour compound in axillary sweat

International Journal of Cosmetic Science

Volumn 33, Issue 3, 2011, Pages 283-286

  Akiba, S ^a   Arai, N ^a   Kusuoku, H ^a   Takagi, Y ^a   Hagura, T ^a   Takeuchi, K ^a   Fuji, A ^a   Fujimura, Tsutomu ^a  

^a KAO CORPORATION   (Japan)

Author keywords

3 hydroxy 3 methyl hexanoic acid; apolipoprotein D; axilla; odour; precursor

Indexed keywords

3 HYDROXYMETHYL 3 METHYLHEXANOIC ACID; APOLIPOPROTEIN D; HEXANOIC ACID DERIVATIVE; TRYPSIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; APOCRINE GLAND; ARTICLE; AXILLA; COVALENT BOND; FEMALE; HUMAN; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NORMAL HUMAN; ODOR; PRECURSOR; PROTEIN ANALYSIS; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SWEAT;

APOLIPOPROTEINS D; AXILLA; BLOTTING, WESTERN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FEMALE; HEXANOIC ACIDS; HUMANS; MOLECULAR WEIGHT; ODORS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SWEAT;

EID: 79955762938     PISSN: 01425463     EISSN: 14682494     Source Type: Journal    
DOI: 10.1111/j.1468-2494.2010.00636.x     Document Type: Article

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