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Processed products of the hevein precursor in the latex of the rubber tree ( Hevea brasiliensis )
Author(s) -
Soedjanaatmadja Ukun M.S.,
Subroto Toto,
Beintema Jaap J.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00309-w
Subject(s) - hevea brasiliensis , proteolysis , natural rubber , hevea , protein precursor , sequence (biology) , complementary dna , chemistry , peptide sequence , biochemistry , organic chemistry , enzyme , gene
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.