Purification of O-acetyl-lserine sulfhydrylase from lens culinaris by affinity chromatography
Joint Authors
Uways, Wajih Musa
Nayifah, Fadwa Kayid
Source
Mutah Journal of Natural, Applied and Health Sciences
Issue
Vol. 8, Issue 5 (31 Dec. 1993), pp.167-185, 19 p.
Publisher
Mutah University Deanship of Scientific Research
Publication Date
1993-12-31
Country of Publication
Jordan
No. of Pages
19
Main Subjects
Abstract EN
O-acetyl-Lserine sulfhydrylase (OASSase) isolated from Lens culinaris was purified (spec.
act.
387 units/mg) to homogeniety using affinity chromatography as a major pu- rificatin step.
The enzyme, Mr = 86,000, consists of two identical subunits, has a pH optimum of 6.4 and is stable to heating up to 50°C.
This enzyme was able in vitro to catalyze the reaction of azide and O-acetylserine to form a mutagenic product on S.
tv phimurium.
Results obtained from double diffusion analysis indicated that the antibody raised against the affinity purified enzyme is monospecific, D-cycloserine, semicrabiazide and hydroxylamine are effective inhibitors of OAS¬Sase activity which is completely inhibited by iodoacetic acid.
American Psychological Association (APA)
Uways, Wajih Musa& Nayifah, Fadwa Kayid. 1993. Purification of O-acetyl-lserine sulfhydrylase from lens culinaris by affinity chromatography. Mutah Journal of Natural, Applied and Health Sciences،Vol. 8, no. 5, pp.167-185.
https://search.emarefa.net/detail/BIM-397556
Modern Language Association (MLA)
Uways, Wajih Musa& Nayifah, Fadwa Kayid. Purification of O-acetyl-lserine sulfhydrylase from lens culinaris by affinity chromatography. Mutah Journal of Natural, Applied and Health Sciences Vol. 8, no. 5 (Dec. 1993), pp.167-185.
https://search.emarefa.net/detail/BIM-397556
American Medical Association (AMA)
Uways, Wajih Musa& Nayifah, Fadwa Kayid. Purification of O-acetyl-lserine sulfhydrylase from lens culinaris by affinity chromatography. Mutah Journal of Natural, Applied and Health Sciences. 1993. Vol. 8, no. 5, pp.167-185.
https://search.emarefa.net/detail/BIM-397556
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references : p. 183-185
Record ID
BIM-397556