Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)
Material type:
TextPublication details: FEBS Letters 1995Description: 211-213Subject(s): Online resources: Summary: The 20-kDa precursor of hevein and its C-terminal 14-kDa domain were isolated. Sequence analysis of the C-terminal tryptic peptides of these proteins and comparison with the cDNA sequence indicated that they represented mature forms from which a C-terminal propeptide, possibly involved in vacuolar targeting, had been removed. The molar ration 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.
| Item type | Current library | Vol info | Status | |
|---|---|---|---|---|
Journals
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RRII Library Physiology | Volume 363, Issue 3 | Journals |
Source Year: 1996
The 20-kDa precursor of hevein and its C-terminal 14-kDa domain were isolated. Sequence analysis of the C-terminal tryptic peptides of these proteins and comparison with the cDNA sequence indicated that they represented mature forms from which a C-terminal propeptide, possibly involved in vacuolar targeting, had been removed. The molar ration 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.
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