Substrate specificity of king cobra (Ophiophagus hannah) VENOM l-amino acid oxidase
1. 1. Substrate specificity of purified king cobra (Ophiophagus hannah) venom l-amino acid oxidase was investigated. 2. 2. The enzyme was highly specific for the l-enantiomer of amino acid. Effective oxidation of l-amino acid by the enzyme requires the presence of a free primary α-amino group but th...
Saved in:
Main Authors: | Nget-Hong, T., Saifuddin, M.N. |
---|---|
Format: | Article |
Language: | en_US |
Published: |
2017
|
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Cytotoxicity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase
by: Lee, M.L., et al.
Published: (2010) -
Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom
by: Tan, N.H., et al.
Published: (2017) -
Enzymatic and toxic properties of Ophiophagus hannah (king cobra) venom and venom fractions
by: Tan, N.-H., et al.
Published: (2017) -
Isolation and characterization of a hemorrhagin from the venom of Ophiophagus hannah (king cobra)
by: Tan, N.H., et al.
Published: (2017) -
Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom
by: Nget-Hong, T., et al.
Published: (2017)