Format:
Online-Ressource
ISSN:
1437-4315
Content:
Abstract: The major protein allergen of peach (Prunus persica), Pru p1, has recently been identified as a lipid transfer protein (LTP). The complete primary structure of Pru p1, obtained by direct amino acid sequence and liquid chromatography-mass spectrometry (LC-MS) analyses with the purified protein, is described here. The protein consists of 91 amino acids with a calculated molecular mass of 9178 Da. The amino acid sequence contains eight strictly conserved cysteines, as do all known LTPs, but secondary structure predictions failed to classify the peach 9 kDa protein as an ‘all-alpha type’, due to the high frequency of amino acids (nine prolines) disrupting alpha helices. Although the sequence similarity with maize LTP is only 63%, out of the 25 amino acids forming the inner surface of the tunnel-like hydrophobic cavity in maize ns-LTP 16 are identical and 7 similar in the peach homolog, supporting the hypothesis of a similar function.
In:
volume:380
In:
number:11
In:
year:1999
In:
pages:1315-1320
In:
Biological chemistry, Berlin [u.a.] : de Gruyter, 1996-, 380, Heft 11 (1999), 1315-1320, 1437-4315
Language:
English
URN:
urn:nbn:de:101:1-2406111601501.054851071771
URL:
https://doi.org/10.1515/BC.1999.167
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2406111601501.054851071771
URL:
https://d-nb.info/1332676898/34
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