Abstract:
:A proteinase present in intercellular wash fluids from leaves of Glycine max has been purified 600-fold to electrophoretic homogeneity. The native protein is monomeric with a molecular mass of 60 kD, as estimated by denaturing gel electrophoresis, and has an isoelectric point of 7.7. The enzyme has a pH optimum of 9.5 when assayed with Azocoll as a substrate. The proteolytic activity is inhibited by p-chloromercuribenzoic acid and mercuric chloride and requires the presence of reducing agents. The enzyme activity is refractory to other classical sulfhydryl proteinases. The soybean leaf endoproteinase is present within the extracellular space of young leaves, and a portion is bound to the cell wall. Western blot analysis and activity measurements show that the enzyme is present only during the first 15 d postemergence of the leaf and is therefore under strict developmental control. We suggest that the enzyme may play a critical role in the extracellular milieu during rapid cell growth and leaf expansion.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Huangpu J,Graham JSdoi
10.1104/pp.108.3.969subject
Has Abstractpub_date
1995-07-01 00:00:00pages
969-974issue
3eissn
0032-0889issn
1532-2548pii
108/3/969journal_volume
108pub_type
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