000			01960nam a2200217Ia 4500
008			220216s9999 xx 000 0 und d
100			_aSubroto T
245		0	_aChitinase and B-1,3-glucanase in the lutoid-body fraction of Hevea latex
260			_bPhytochemistry _c1996
300			_a29-37
500			_aSource Year: 1997
520			_aThe lutoid-body fraction of latex from Hevea brasiliensis contains a limited number of major proteins (hevein, its precursor and the C-terminal fragment of this precursor, proteins with enzymic activities : 3 hevamine components, which are basic, vacuolar, chitinases with lysozyme activity, and a B-1,3-glucanase). Lutoid-body fractions from 3 clones (GT 1, PR 261 and LCB 1320) differed in their contents of these proteins. The hevamine components and glucanase were isolated and several enzymic and structural properties were investigated. These enzymes are basic proteins that cause coagulation of the negatively charged rubber particles. The coagulation occures in a rather narrow range of ratios of added protein to rubber particles, which indicates that charge neutralization is the determining factor. Differences in coagulation of rubber particles by lutoid-body fractions from different clones can be explained by their content of hevamine and glucanase. Glucanase from the lutoid-body fraction may dissolve callus tissue and this may explain the observation that clones with a high glucanase content produce more latex than clones with little glucanase. Sequence studies of 2CNBr peptides of the glucanase indicate that this protein is homologous with glucanase from other plants, and that a C-terminal peptide, possibly involved in vacuolar targeting, may have been cleaved off.
650			_aHevea brasiliensis
650			_aHevea latex
700			_aBeintema J J
700			_aKoningsveld G A van
700			_aSchreuder H A
700			_aSoedjanaatmadja U M S
856			_uIRRDB
942			_cJS
999			_c55562 _d55562