Open AccessPurification of a Trypsin Inhibitor Secreted by Embryogenic Carrot Cells
Author(s) -
Irene Carlberg,
Lisbeth Jonsson,
Annika Bergenstråhle,
Kenneth Söderhäll
Publication year - 1987
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.84.1.197
Subject(s) - daucus carota , trypsin inhibitor , trypsin , subtilisin , biochemistry , kunitz sti protease inhibitor , protease inhibitor (pharmacology) , protease , biology , lysis , enzyme inhibitor , cell culture , microbiology and biotechnology , enzyme , chemistry , botany , genetics , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load , immunology
A protease inhibitor with a molecular weight of about 12,800 was purified to electrophoretic homogeneity from Daucus carota cells. The protease inhibitor was heat stable and inhibited trypsin but had no activity toward chymotrypsin or subtilisin. Nonembryogenic as well as embryogenic strains contained the inhibitor in similar amounts, but in the embryogenic strains the trypsin inhibitor was released from the cells and as a result accumulated in high concentrations in the culture medium, whereas no release of the trypsin inhibitor was found during cultivation of the nonembryogenic strains. Very low amounts of acid phosphatase or alpha-mannosidase activity were found in the culture filtrate of both embryogenic and nonembryogenic strains, which suggest that the release of the inhibitor from embryogenic strains was not due to cell lysis.
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