Purification and Developmental Analysis of an Extracellular Proteinase from Young Leaves of Soybean.

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 Physiol

journal_title

Plant physiology

authors

Huangpu J,Graham JS

doi

10.1104/pp.108.3.969

subject

Has Abstract

pub_date

1995-07-01 00:00:00

pages

969-974

issue

3

eissn

0032-0889

issn

1532-2548

pii

108/3/969

journal_volume

108

pub_type

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