title: Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis).
abstract: The 20 kDa precursor of hevein and its C-terminal 14 kDa domain have been isolated. Sequence analysis of the C-terminal tryptic peptides of these proteins and comparison with the cDNA sequence indicate that they represent mature forms from which a C-terminal propeptide, possibly involved in vacuolar targeting, has been removed. The molar ratio of hevein to the C-terminal domain in the lutoid-body fraction of rubber latex is about 30:1. This indicates that not only the pre- and propeptides but also the 14 kDa domain are removed by proteolysis or other processes in the latex vessel after the processing of hevein has taken place.
authors.affiliation: Laboratorium Biokimia, FMIPA, Universitas Padjadjaran, Bandung, Indonesia.
authors.forename: U M
authors.initials: UM
authors.lastname: Soedjanaatmadja
authors.forename: T
authors.initials: T
authors.lastname: Subroto
authors.forename: J J
authors.initials: JJ
authors.lastname: Beintema
mesh_terms: D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides; D007840:Latex / Q000737:chemistry; D037102:Lectins / Q000378:metabolism*; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010940:Plant Proteins / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014197:Trees
chemical_list: D023181:Antimicrobial Cationic Peptides; D007840:Latex; D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; D011498:Protein Precursors; C045875:hevein