Purification and Characterization of Two Benzoyl-l-Tyrosine p-Nitroanilide Hydrolases from Etiolated Leaves of Zea mays L.

Abstract:

:Two benzoyl-l-tyrosine p-nitroanilide hydrolases (BTPAases I and II) were purified from the etiolated leaves of Zea mays L. and characterized. BTPAase I was electrophoretically homogeneous and consisted of two identical subunits having a molecular weight of 53,000. The molecular weight of BTPAase II was 65,000. The Michaelis constants for substrate, BTPA, were 4 millimolar and 1.3 millimolar for BTPAases I and II, respectively. Based on the action of various inhibitors on both enzyme activities, these enzymes were classified as serine proteases. BTPAase I showed caseinolytic activity at neutral pH and the activity was strongly inhibited by the serine protease inhibitors.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Doi M,Shioi Y

doi

10.1104/pp.84.3.770

subject

Has Abstract

pub_date

1987-07-01 00:00:00

pages

770-4

issue

3

eissn

0032-0889

issn

1532-2548

journal_volume

84

pub_type

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