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Partial Purification and Characterization of Proteases in Tobacco Leaf and Callus
1984
Beiträge zur Tabakforschung International
Ammonium sulfate fra.ctionation, gel permeation and cation-exchange column chromatography were employed for panial purification of proteases from leaf laminae and callus tissues of Samsun NN tobacco (Nicotiana tabacum L). The predominant proteases in the leaf and callus are acidic sulfhydryl proteases which are activated by 2-mercaptoethanol and ethylenediamine tetraacetic acid, completely inhibited- by iodoacetic acid, and partially inhibited by phenylmethane sulfonyl fluoride and pepstatin A.
doi:10.2478/cttr-2013-0543
fatcat:eul6nykgx5gonek3rm6cnbcah4