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 Physioljournal_title
Plant physiologyauthors
Doi M,Shioi Ydoi
10.1104/pp.84.3.770subject
Has Abstractpub_date
1987-07-01 00:00:00pages
770-4issue
3eissn
0032-0889issn
1532-2548journal_volume
84pub_type
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