Demonstration by mass spectrometry that pseudo-hevein and hevein have ragged C-terminal sequences.
The primary structure of pseudo-hevein, a minor hevein component from the latex of the rubber tree, Hevea brasiliensis, was determined. Six differences with the sequence of the major hevein component were found, one of which is a replacement of tryptophan by tyrosine in the carbohydrate binding region of the molecule. Analysis by ion-spray mass spectrometry showed that pseudo-hevein has a heterogeneous C-terminal extension of several glycine residues and that hevein itself also contains minor components with additional C-terminal amino-acid residues. A seventh difference between the two sequences occurs in these extensions.
Soedjanaatmadja
U M
UM
Biochemical Laboratory, FMIPA, University Padjadjara, Indonesia.
Hofsteenge
J
J
Jeronimus-Stratingh
C M
CM
Bruins
A P
AP
Beintema
J J
JJ
D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides; D037102:Lectins / Q000737:chemistry*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010940:Plant Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D014197:Trees / Q000737:chemistry
D023181:Antimicrobial Cationic Peptides; D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; C090618:pseudohevein; C045875:hevein