TY - JOUR
T1 - Complete amino acid sequence determination of the major allergen of peach (Prunus persica) Pru p 1
AU - Pastorello, Elide A.
AU - Ortolani, Claudio
AU - Baroglio, Chiara
AU - Pravettoni, Valerio
AU - Ispano, Marco
AU - Giuffrida, Maria Gabriella
AU - Fortunato, Donatella
AU - Farioli, Laura
AU - Monza, Mara
AU - Napolitano, Lorenzo
AU - Sacco, Marco
AU - Scibola, Elisabetta
AU - Conti, Amedeo
PY - 1999/11
Y1 - 1999/11
N2 - The major protein allergen of peach (Prunus persica), Pru p 1, has recently been identified as a lipid transfer protein (LTP). The complete primary structure of Pru p 1, 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.
AB - The major protein allergen of peach (Prunus persica), Pru p 1, has recently been identified as a lipid transfer protein (LTP). The complete primary structure of Pru p 1, 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.
KW - Lipid transfer protein
KW - Primary structure
KW - Rosaceae
UR - http://www.scopus.com/inward/record.url?scp=0032754269&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032754269&partnerID=8YFLogxK
M3 - Article
C2 - 10614824
AN - SCOPUS:0032754269
VL - 380
SP - 1315
EP - 1320
JO - Biological Chemistry
JF - Biological Chemistry
SN - 1431-6730
IS - 11
ER -