Partial purification of metalloprotease from acacia farnesiana
Other Title(s)
تنقية جزئية لأنزيم البروتيزالمعدني المستخلص من نبات شوك الشام Acacia farnesiana
Joint Authors
Sahib, Muhannad Muhammad
Hamzah, Nizar Abd al-Amir
Source
al-Kufa University Journal for Biology
Issue
Vol. 7, Issue 1 (30 Jun. 2015)9 p.
Publisher
University of Kufa Faculty of Science Department of live Sciences
Publication Date
2015-06-30
Country of Publication
Iraq
No. of Pages
9
Main Subjects
Topics
Abstract AR
Not previously studied metalloprotease was tested in four species of leguminosae, purified and characterized from Acacia farnesiana which have maximum specific activity 25.01 U/mg.
Precipitation by 50% ammonium sulfate referred to increase of specific activity (35.84) U/mg while loading on DEAE-Cellulose exchanger pointed out elevation of specific activity and purification fold, 51.39 unit/mg and 2.06 respectively.
Molecular mass, pH and temperature optima of purified metalloprotease were 55.11kDa, 7.5 and 50oC respectively.
All metal ions were decreased enzyme activity except the zinc showed the increasing about 16%.
EDTA was inhibiting the activity in otherwise other inhibitor not affected on enzyme activity.
Optimum substrate for activity was BSA and has Km and Vmax 1.11mM and 625 mM/ min respectively.
Abstract EN
Not previously studied metalloprotease was tested in four species of leguminosae, purified and characterized from Acacia farnesiana which have maximum specific activity 25.01 U/mg.
Precipitation by 50% ammonium sulfate referred to increase of specific activity (35.84) U/mg while loading on DEAE-Cellulose exchanger pointed out elevation of specific activity and purification fold, 51.39 unit/mg and 2.06 respectively.
Molecular mass, pH and temperature optima of purified metalloprotease were 55.11kDa, 7.5 and 50oC respectively.
All metal ions were decreased enzyme activity except the zinc showed the increasing about 16%.
EDTA was inhibiting the activity in otherwise other inhibitor not affected on enzyme activity.
Optimum substrate for activity was BSA and has Km and Vmax 1.11mM and 625 mM/ min respectively.
American Psychological Association (APA)
Hamzah, Nizar Abd al-Amir& Sahib, Muhannad Muhammad. 2015. Partial purification of metalloprotease from acacia farnesiana. al-Kufa University Journal for Biology،Vol. 7, no. 1.
https://search.emarefa.net/detail/BIM-594271
Modern Language Association (MLA)
Hamzah, Nizar Abd al-Amir& Sahib, Muhannad Muhammad. Partial purification of metalloprotease from acacia farnesiana. al-Kufa University Journal for Biology Vol. 7, no. 1 (2015).
https://search.emarefa.net/detail/BIM-594271
American Medical Association (AMA)
Hamzah, Nizar Abd al-Amir& Sahib, Muhannad Muhammad. Partial purification of metalloprotease from acacia farnesiana. al-Kufa University Journal for Biology. 2015. Vol. 7, no. 1.
https://search.emarefa.net/detail/BIM-594271
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-594271
