Distribution of proteinase inhibitors in seeds of Australian acacias [wattles]
1981
Weder, J.K.P. | Murray, D.R. (Technische Univ. Muenchen (Germany, F.R.). Inst. fuer Lebensmittelchemie)
Extracts from seeds of 38 Australian Acacia species inhibit trypsin and with one exception also alpha-chymotrypsin. Inhibitory activities lay between 0.3 and 6.1 mg of trypsin and 0.1 and 6.3 mg of alpha-chymotrypsin, respectively, (TI) and chymotrypsin inhibitors (CTI) after disc electrophoresis results in three different types of inhibitor patterns: with all ITI bands being of greater anodic electrophoretic mobility than the TI bands (type A), with CTI bands being of both equal and greater mobility than the TI bands (type B), and with CTI and TI bands being of equal mobility (type C). The TI and CTI activities, the quotients of the two activities, and/or the types of inhibitor patterns indicate closer relationships between uninerved Racemosae (A) and Botryocephalae (Bipinnatae) (A) as well as between Plurinerves (mostly B) and Pulchellae (Bipinnatae) (B), than between the two Bipinnatae or between Plurinerves and Juliflorae.
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