Friday, February 11, 2011

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

Synopsis

Axillary sweat is odourless when freshly collected at the surface of human skin, but it contains non-odoriferous precursors, which can be transformed into odorous substances by bacteria. E-3-methyl-2-hexanoic acid (3M2H) is one of the key odorous substances, but there are two contradictory reports about its precursor form. One report states that 3M2H linked non-covalently to apolipoprotein D (apoD) is the precursor, while a second report states that 3M2H–Gln identified in human axillary sweat is the precursor. Recently, 3-hydroxy-3-methyl hexanoic acid (HMHA) and 3-methyl-3-sulfanylhexane-1-ol (3M3T) have also been identified and reported ...

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 is a post from: Skincare




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 via BuzzBlazer.com

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