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Purification and properties of asparaginase from the testa of immature seeds of pea (Pisum sativum L.) BABT
Chagas,Eliana P.; Sodek,Ladaslav.
A K+-dependent asparaginase (E.C. 3.5.1.1.) was purified 1328-fold from the testas of immature pea seeds (Pisum sativum L., var. Bolero) and characterized. Antibodies raised against purified asparaginase cross-reacted with the putative asparaginase band in Western blot analyses of semi-purified extracts. However, for crude extracts of pea testas, a cross-reaction was obtained with at least four protein bands, one of which was asparaginase protein. Affinity-purified antibodies to the four strongest bands of crude extracts were fairly specific for the bands from which they were purified, suggesting a mixture of specific antibodies. The Mr of asparaginase was 69,000 by Sephacryl S200 chromatography and also by mobility on native PAGE relative to BSA. There...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Pisum sativum; Asparaginase; Purification; Properties.
Ano: 2001 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132001000300004
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