Purification and characterization of cathepsin D from the lizard Agama stellio stellio
Joint Authors
al-Jassabi, Sad
Abu Ghalyun, Yunus
Source
Issue
Vol. 4, Issue 2 (31 Jul. 1999), pp.247-258, 12 p.
Publisher
Al al-Bayt University Deanship of Academic Research and Graduate Studies
Publication Date
1999-07-31
Country of Publication
Jordan
No. of Pages
12
Main Subjects
Topics
Abstract EN
Cathepsin D was isolated from the lizard Agama stellio stellio skeletal muscle and purified to electrophoretical homogeneity for the first time in lizards species by concanavalin A-sepharose and sephadex G-100 chromatographies Purified cathepsin D from skeletal muscle of this lizard appeared to be electrophoretically homogenous and had a molecular weight of 6400 Daltons estimated by sephadex G-100 and 67000 Daltons by SDS-PAGE.
This enzyme was completely inhibited by.
Pepstatin, Hg2+, and Fe3+ and was partially inhibited by phenyl methyl sulfonyl florid (PMSF) P-chloromercuribenzoate (PCMB).
SDS, and iodoacetic acid.
(IAA).
The PI of this enzyme was 5.13, and the optimal pH and temperature were 3.5 and 37ْ C respectively.
American Psychological Association (APA)
al-Jassabi, Sad& Abu Ghalyun, Yunus. 1999. Purification and characterization of cathepsin D from the lizard Agama stellio stellio. Al-Manarah،Vol. 4, no. 2, pp.247-258.
https://search.emarefa.net/detail/BIM-169221
Modern Language Association (MLA)
al-Jassabi, Sad& Abu Ghalyun, Yunus. Purification and characterization of cathepsin D from the lizard Agama stellio stellio. Al-Manarah Vol. 4, no. 2 (Jul. 1999), pp.247-258.
https://search.emarefa.net/detail/BIM-169221
American Medical Association (AMA)
al-Jassabi, Sad& Abu Ghalyun, Yunus. Purification and characterization of cathepsin D from the lizard Agama stellio stellio. Al-Manarah. 1999. Vol. 4, no. 2, pp.247-258.
https://search.emarefa.net/detail/BIM-169221
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references : p. 257-258
Record ID
BIM-169221
