Isolation of a protease active at neutral pH with a molecular mass of 65 kDa from the lutoid-body fraction of Hevea brasiliensis latex
Material type:
TextPublication details: Journal of Rubber Research 2003Description: 48-57Subject(s): Summary: A protease with molecular mass of 65 kDa was isolated from the lutoid-body (vacuolar) fraction of latex of the rubber tree, Hevea brasiliensis, and assigned to one of the approximately ten protein bands visible on SDS-PAGE patterns of this fraction. The enzyme had an optimum activity at pH 7.4 and was inhibited at this and higher pH values in the cytosol fraction of rubber latex. There might be a small proteolytic activity at the low internal pH of lutoid-bodies. The 19 kDa precursor of hevein disappeared during incubation of lutoid-body preparations at neurtal pH, but not at lower pH. A possible general role of the 65 kDa protease in processing of vacuolar proteins needs more investigation.
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RRII Library Physiology | Volume 6, Issue 1 | Journals |
A protease with molecular mass of 65 kDa was isolated from the lutoid-body (vacuolar) fraction of latex of the rubber tree, Hevea brasiliensis, and assigned to one of the approximately ten protein bands visible on SDS-PAGE patterns of this fraction. The enzyme had an optimum activity at pH 7.4 and was inhibited at this and higher pH values in the cytosol fraction of rubber latex. There might be a small proteolytic activity at the low internal pH of lutoid-bodies. The 19 kDa precursor of hevein disappeared during incubation of lutoid-body preparations at neurtal pH, but not at lower pH. A possible general role of the 65 kDa protease in processing of vacuolar proteins needs more investigation.
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