PMID- 11368308
OWN - NLM
STAT- MEDLINE
DCOM- 20010614
LR  - 20061115
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 384
IP  - 2
DP  - 2000 Dec 15
TI  - Isolation, structural, and functional characterization of an apoptosis-inducing 
      L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom.
PG  - 216-26
AB  - The enzyme L-amino acid oxidase (LAO) from the leaf-nosed viper (Eristocophis 
      macmahoni) snake venom was purified to homogeneity in a single step using high 
      performance liquid chromatography on a Nucleosil 7C18 reverse phase column. The 
      molecular mass of the purified enzyme was 58734.0 Da, as determined by 
      matrix-assisted laser desorption/ionization mass spectrometry. The N-terminal 
      amino acid sequence (ADDKNPLEEAFREADYEVFLEIAKNGL) and the chemical composition of 
      the purified LNV-LAO shows close structural homology with other L-amino acid 
      oxidases isolated from different snake venoms. The secondary structural contents 
      analysis of LAO, established by means of circular dichroism, revealed ca. 49% 
      alpha-helix, 19% beta-sheet, 10% beta-turn, and 22% random coil structure. The 
      purified LNV-LAO not only retained its specific enzymatic activity (73.46 U/mg), 
      determined against L-leucine as a substrate, but also exhibited potent haemolytic 
      (1-10 microg/ml), edema- (MED 4.8 microg/ml) and human platelet 
      aggregation-inducing (ED50 33 microg/ml) properties. Unlike other haemorrhagic 
      snake venom L-amino acid oxidases, the LNV-LAO does not produce haemorrhage. In 
      addition to these local effects, the purified LNV-LAO showed apoptosis-inducing 
      activity in the MM6 cell culture assay. After 18 h treatment with 25-100 
      microg/ml of LAO, the typical DNA fragmentation pattern of apoptotic cells was 
      observed by means of fluorescent microscopy and agarose gel electrophoresis.
FAU - Ali, S A
AU  - Ali SA
AD  - International Center for Chemical Sciences, HEJ Research Institute of Chemistry, 
      University of Karachi, Pakistan. saali66@hotmail.com
FAU - Stoeva, S
AU  - Stoeva S
FAU - Abbasi, A
AU  - Abbasi A
FAU - Alam, J M
AU  - Alam JM
FAU - Kayed, R
AU  - Kayed R
FAU - Faigle, M
AU  - Faigle M
FAU - Neumeister, B
AU  - Neumeister B
FAU - Voelter, W
AU  - Voelter W
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Viper Venoms)
RN  - EC 1.4.- (Amino Acid Oxidoreductases)
RN  - EC 1.4.3.2 (L-Amino Acid Oxidase)
SB  - IM
MH  - Amino Acid Oxidoreductases/*chemistry/isolation & purification/*pharmacology
MH  - Amino Acid Sequence
MH  - Animals
MH  - Apoptosis/*drug effects
MH  - Cell Line
MH  - Cell Nucleus/ultrastructure
MH  - Chromatography, High Pressure Liquid
MH  - DNA Fragmentation
MH  - Edema/chemically induced
MH  - Hemolysis/drug effects
MH  - Hemorrhage/chemically induced
MH  - Humans
MH  - L-Amino Acid Oxidase
MH  - Mice
MH  - Molecular Sequence Data
MH  - Platelet Aggregation/drug effects
MH  - Protein Structure, Secondary
MH  - Sequence Homology, Amino Acid
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Structure-Activity Relationship
MH  - Viper Venoms/*enzymology
EDAT- 2001/05/23 10:00
MHDA- 2001/06/23 10:01
CRDT- 2001/05/23 10:00
PHST- 2001/05/23 10:00 [pubmed]
PHST- 2001/06/23 10:01 [medline]
PHST- 2001/05/23 10:00 [entrez]
AID - S0003-9861(00)92130-1 [pii]
AID - 10.1006/abbi.2000.2130 [doi]
PST - ppublish
SO  - Arch Biochem Biophys. 2000 Dec 15;384(2):216-26. doi: 10.1006/abbi.2000.2130.