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  1. Article ; Online: Analysis of the efficacy of Taiwanese freeze-dried neurotoxic antivenom against Naja kaouthia, Naja siamensis and Ophiophagus hannah through proteomics and animal model approaches.

    Liu, Chien-Chun / You, Chen-Hsien / Wang, Po-Jung / Yu, Jau-Song / Huang, Guo-Jen / Liu, Chien-Hsin / Hsieh, Wen-Chin / Lin, Chih-Chuan

    PLoS neglected tropical diseases

    2017  Volume 11, Issue 12, Page(s) e0006138

    Abstract: ... kaouthia (Thailand) and Naja siamensis (Thailand), and the king cobra Ophiophagus hannah (Indonesia ... but not O. hannah venom. MS-based venom protein identification results further revealed that FNAV strongly ...

    Abstract In Southeast Asia, envenoming resulting from cobra snakebites is an important public health issue in many regions, and antivenom therapy is the standard treatment for the snakebite. Because these cobras share a close evolutionary history, the amino acid sequences of major venom components in different snakes are very similar. Therefore, either monovalent or polyvalent antivenoms may offer paraspecific protection against envenomation of humans by several different snakes. In Taiwan, a bivalent antivenom-freeze-dried neurotoxic antivenom (FNAV)-against Bungarus multicinctus and Naja atra is available. However, whether this antivenom is also capable of neutralizing the venom of other species of snakes is not known. Here, to expand the clinical application of Taiwanese FNAV, we used an animal model to evaluate the neutralizing ability of FNAV against the venoms of three common snakes in Southeast Asia, including two 'true' cobras Naja kaouthia (Thailand) and Naja siamensis (Thailand), and the king cobra Ophiophagus hannah (Indonesia). We further applied mass spectrometry (MS)-based proteomic techniques to characterize venom proteomes and identify FNAV-recognizable antigens in the venoms of these Asian snakes. Neutralization assays in a mouse model showed that FNAV effectively neutralized the lethality of N. kaouthia and N. siamensis venoms, but not O. hannah venom. MS-based venom protein identification results further revealed that FNAV strongly recognized three-finger toxin and phospholipase A2, the major protein components of N. kaouthia and N. siamensis venoms. The characterization of venom proteomes and identification of FNAV-recognizable venom antigens may help researchers to further develop more effective antivenom designed to block the toxicity of dominant toxic proteins, with the ultimate goal of achieving broadly therapeutic effects against these cobra snakebites.
    MeSH term(s) Animals ; Antidotes/chemistry ; Antidotes/pharmacology ; Antivenins/chemistry ; Antivenins/pharmacology ; Chromatography, High Pressure Liquid ; Chromatography, Liquid ; Disease Models, Animal ; Elapid Venoms/chemistry ; Elapid Venoms/poisoning ; Freeze Drying ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Neutralization Tests ; Proteome ; Snake Bites/drug therapy ; Taiwan ; Tandem Mass Spectrometry
    Chemical Substances Antidotes ; Antivenins ; Elapid Venoms ; Proteome
    Language English
    Publishing date 2017
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2429704-5
    ISSN 1935-2735 ; 1935-2727
    ISSN (online) 1935-2735
    ISSN 1935-2727
    DOI 10.1371/journal.pntd.0006138
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Analysis of the efficacy of Taiwanese freeze-dried neurotoxic antivenom against Naja kaouthia, Naja siamensis and Ophiophagus hannah through proteomics and animal model approaches.

    Chien-Chun Liu / Chen-Hsien You / Po-Jung Wang / Jau-Song Yu / Guo-Jen Huang / Chien-Hsin Liu / Wen-Chin Hsieh / Chih-Chuan Lin

    PLoS Neglected Tropical Diseases, Vol 11, Iss 12, p e

    2017  Volume 0006138

    Abstract: ... kaouthia (Thailand) and Naja siamensis (Thailand), and the king cobra Ophiophagus hannah (Indonesia ... but not O. hannah venom. MS-based venom protein identification results further revealed that FNAV strongly ...

    Abstract In Southeast Asia, envenoming resulting from cobra snakebites is an important public health issue in many regions, and antivenom therapy is the standard treatment for the snakebite. Because these cobras share a close evolutionary history, the amino acid sequences of major venom components in different snakes are very similar. Therefore, either monovalent or polyvalent antivenoms may offer paraspecific protection against envenomation of humans by several different snakes. In Taiwan, a bivalent antivenom-freeze-dried neurotoxic antivenom (FNAV)-against Bungarus multicinctus and Naja atra is available. However, whether this antivenom is also capable of neutralizing the venom of other species of snakes is not known. Here, to expand the clinical application of Taiwanese FNAV, we used an animal model to evaluate the neutralizing ability of FNAV against the venoms of three common snakes in Southeast Asia, including two 'true' cobras Naja kaouthia (Thailand) and Naja siamensis (Thailand), and the king cobra Ophiophagus hannah (Indonesia). We further applied mass spectrometry (MS)-based proteomic techniques to characterize venom proteomes and identify FNAV-recognizable antigens in the venoms of these Asian snakes. Neutralization assays in a mouse model showed that FNAV effectively neutralized the lethality of N. kaouthia and N. siamensis venoms, but not O. hannah venom. MS-based venom protein identification results further revealed that FNAV strongly recognized three-finger toxin and phospholipase A2, the major protein components of N. kaouthia and N. siamensis venoms. The characterization of venom proteomes and identification of FNAV-recognizable venom antigens may help researchers to further develop more effective antivenom designed to block the toxicity of dominant toxic proteins, with the ultimate goal of achieving broadly therapeutic effects against these cobra snakebites.
    Keywords Arctic medicine. Tropical medicine ; RC955-962 ; Public aspects of medicine ; RA1-1270
    Subject code 616
    Language English
    Publishing date 2017-12-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Structure of a cardiotoxic phospholipase A(2) from Ophiophagus hannah with the "pancreatic loop".

    Zhang, Hai-Long / Xu, Su-Juan / Wang, Qiu-Yan / Song, Shi-Ying / Shu, Yu-Yan / Lin, Zheng-Jiong

    Journal of structural biology

    2002  Volume 138, Issue 3, Page(s) 207–215

    Abstract: The crystal structure of an acidic phospholipase A(2) from Ophiophagus hannah (king cobra) has been ...

    Abstract The crystal structure of an acidic phospholipase A(2) from Ophiophagus hannah (king cobra) has been determined by molecular replacement at 2.6-A resolution to a crystallographic R factor of 20.5% (R(free)=23.3%) with reasonable stereochemistry. The venom enzyme contains an unusual "pancreatic loop." The conformation of the loop is well defined and different from those in pancreas PLA(2), showing its structural variability. This analysis provides the first structure of a PLA(2)-type cardiotoxin. The sites related to the cardiotoxic and myotoxic activities are explored and the oligomer observed in the crystalline state is described.
    MeSH term(s) Amino Acid Sequence ; Animals ; Binding Sites ; Cobra Cardiotoxin Proteins/chemistry ; Crystallography, X-Ray ; Elapidae/metabolism ; Electrons ; Models, Molecular ; Molecular Sequence Data ; Phospholipases A/chemistry ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Structure-Activity Relationship
    Chemical Substances Cobra Cardiotoxin Proteins ; Phospholipases A (EC 3.1.1.32)
    Language English
    Publishing date 2002-09-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1032718-6
    ISSN 1095-8657 ; 1047-8477
    ISSN (online) 1095-8657
    ISSN 1047-8477
    DOI 10.1016/s1047-8477(02)00022-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Preliminary crystallographic study of an acidic phospholipase A2 from Ophiophagus hannah (king cobra).

    Xu, Sujuan / Gu, Lichuan / Wang, Qiuyan / Shu, Yuyan / Lin, Zhengjiong

    Acta crystallographica. Section D, Biological crystallography

    2002  Volume 58, Issue Pt 10 Pt 2, Page(s) 1836–1837

    Abstract: ... isolated from Ophiophagus hannah (king cobra) from Guangxi province, China. Comparison of this enzyme ...

    Abstract An acidic phospholipase A(2) (OH APLA(2)-II) with an isoelectric point (pI) of 4.0 was recently isolated from Ophiophagus hannah (king cobra) from Guangxi province, China. Comparison of this enzyme to a previously reported homologous phospholipase A(2) from the same venom shows that it lacks toxicity and exhibits a greater phospholipase activity. OH APLA(2)-II has been crystallized by the hanging-drop vapour-diffusion method using 1,6-hexanediol and magnesium chloride as precipitants. The crystal belongs to space group P6(3), with unit-cell parameters a = b = 98.06, c = 132.39 A. The diffraction data were collected under cryoconditions (100 K) and reduced to 2.1 A resolution. A molecular-replacement solution has been determined and shows that there are six molecules in one asymmetric unit.
    MeSH term(s) Animals ; China ; Crystallography, X-Ray/methods ; Elapid Venoms/chemistry ; Elapid Venoms/isolation & purification ; Elapidae ; Kinetics ; Phospholipases A/chemistry ; Phospholipases A/isolation & purification ; Phospholipases A2
    Chemical Substances Elapid Venoms ; Phospholipases A (EC 3.1.1.32) ; Phospholipases A2 (EC 3.1.1.4)
    Language English
    Publishing date 2002-09-28
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2968623-4
    ISSN 2059-7983 ; 0907-4449
    ISSN (online) 2059-7983
    ISSN 0907-4449
    DOI 10.1107/s0907444902011654
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Crystallization and preliminary X-ray analysis of cardiotoxic phospholipase A2 from Ophiophagus hannah (king cobra).

    Wang, Z / Zhuang, M / Shu, Y / Zhang, H / Song, S / Lin, Z

    Acta crystallographica. Section D, Biological crystallography

    2001  Volume 57, Issue Pt 5, Page(s) 709–710

    Abstract: ... isolated from Ophiophagus hannah (king cobra) from Guangxi, China. It contains an unusual 'pancreatic loop' ...

    Abstract An acidic phospholipase A2 exhibiting cardiotoxicity, myotoxicity and anti-platelet activity was isolated from Ophiophagus hannah (king cobra) from Guangxi, China. It contains an unusual 'pancreatic loop'. The enzyme was purified to homogeneity and crystallized using polyethylene glycol and ethylene glycol as precipitants. The crystal belongs to space group C2, with unit-cell parameters a = 117.92, b = 62.94, c = 57.16 A, beta = 100.93 degrees. Diffraction data were collected to 2.6 A.
    MeSH term(s) Animals ; Crystallization ; Crystallography, X-Ray ; Elapid Venoms/enzymology ; Elapidae ; Heart/drug effects ; Phospholipases A/chemistry ; Phospholipases A/toxicity ; Phospholipases A2 ; Protein Conformation
    Chemical Substances Elapid Venoms ; Phospholipases A (EC 3.1.1.32) ; Phospholipases A2 (EC 3.1.1.4)
    Language English
    Publishing date 2001-04-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2968623-4
    ISSN 2059-7983 ; 0907-4449
    ISSN (online) 2059-7983
    ISSN 0907-4449
    DOI 10.1107/s0907444901002293
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Characterization of OhS1, an arginine/lysine amidase from the venom of king cobra (Ophiophagus hannah).

    Zhang, Y / Lee, W H / Xiong, Y L / Wang, W Y / Zu, S W

    Toxicon : official journal of the International Society on Toxinology

    1994  Volume 32, Issue 5, Page(s) 615–623

    Abstract: ... amidase from the venom of Ophiophagus hannah (OhS1). It was purified by Sephadex G-75 gel filtration and ...

    Abstract In this paper, we present the results of purification and characterization of an arginine/lysine amidase from the venom of Ophiophagus hannah (OhS1). It was purified by Sephadex G-75 gel filtration and ion-exchange chromatography on DEAE-Sepharose CL-6B. It is a protein of about 43,000, consisting of a single polypeptide chain. It is a minor component in the venom. The purified enzyme was capable of hydrolysing several tripeptidyl-p-nitroanilide substrates having either arginine or lysine as the C-terminal residue. We studied the kinetic parameters of OhS1 on six these chromogenic substrates. OhS1 did not clot fibrinogen. Electrophoresis of fibrinogen degraded with OhS1 revealed the disappearance of the alpha- and beta-chains and the appearance of lower mol. wt fragments. OhS1 had no hemorrhagic activity. It did not hydrolyse casein, nor did it act on blood coagulation factor X, prothrombin and plasminogen. The activity of OhS1 was completely inhibited by NPGB, PMSF, DFP, benzamidine and soybean trypsin inhibitor, suggesting it is a serine protease. Metal chelator (EDTA) had no effect on it.
    MeSH term(s) Amidohydrolases/antagonists & inhibitors ; Amidohydrolases/chemistry ; Amidohydrolases/isolation & purification ; Amidohydrolases/metabolism ; Amino Acid Sequence ; Arginine ; Elapid Venoms/chemistry ; Lysine ; Molecular Sequence Data ; Protease Inhibitors/pharmacology ; Serine Endopeptidases/analysis ; Serine Endopeptidases/chemistry ; Serine Endopeptidases/isolation & purification ; Serine Endopeptidases/metabolism ; Substrate Specificity
    Chemical Substances Elapid Venoms ; Protease Inhibitors ; Arginine (94ZLA3W45F) ; Serine Endopeptidases (EC 3.4.21.-) ; arginine - lysine amidase, Ophiophagus hannah (EC 3.4.21.-) ; Amidohydrolases (EC 3.5.-) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 1994-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/0041-0101(94)90209-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Cloning and Sequence Analysis of cDNAs Encoding Two Acidic PLA(2) from venom of Ophiophagus hannah(King Cobra), Guangxi Species.

    Wang, Qiu-Yan / Shu, Yu-Yan / Zhuang, Mao-Xing / Lin, Zheng-Jiong

    Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica

    2001  Volume 33, Issue 3, Page(s) 340–344

    Abstract: Total RNA was extracted from venom glands of Ophiophagus hannah, Guangxi species. The cDNAs ... hannah, Fujian and Taiwan species, but APLA(2)-2 had lower homology. The most striking difference between ... APLA(2)-2 and other PLA(2) from Ophiophagus hannah venoms is the missing of a extra "pancreatic loop ...

    Abstract Total RNA was extracted from venom glands of Ophiophagus hannah, Guangxi species. The cDNAs encoding PLA(2) were amplified by RT-PCR and cloned into the PUCm-T vector. The positive clones encoding two acidic PLA(2) (APLA(2)-1 and APLA(2)-2) were selected and bidirectionally sequenced. Their complete amino acid sequences were deduced and found to be identical to the known amino acid sequences. Their isoelectric points calculated by computer agreed with the values determined with their protein. Homology analysis indicated that the mature peptide of APLA(2)-1 had high homology with PLA(2) from venoms of Ophiophagus hannah, Fujian and Taiwan species, but APLA(2)-2 had lower homology. The most striking difference between APLA(2)-2 and other PLA(2) from Ophiophagus hannah venoms is the missing of a extra "pancreatic loop" at residues 62--66 in APLA(2)-2, and it may be related to their species evolution and biological activity.
    Language English
    Publishing date 2001
    Publishing country China
    Document type Journal Article
    ZDB-ID 2175256-4
    ISSN 1745-7270 ; 0582-9879 ; 1672-9145
    ISSN (online) 1745-7270
    ISSN 0582-9879 ; 1672-9145
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Isolation and properties of a blood coagulation factor X activator from the venom of king cobra (Ophiophagus hannah).

    Lee, W H / Zhang, Y / Wang, W Y / Xiong, Y L / Gao, R

    Toxicon : official journal of the International Society on Toxinology

    1995  Volume 33, Issue 10, Page(s) 1263–1276

    Abstract: A specific blood coagulation factor X activator was purified from the venom of Ophiophagus hannah ... These results suggest that the factor X activator from O. hannah venom is a serine protease. ...

    Abstract A specific blood coagulation factor X activator was purified from the venom of Ophiophagus hannah by gel filtration and two steps of FPLC Mono-Q column ion-exchange chromatography. It showed a single protein band both in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and alkaline polyacrylamide gel electrophoresis. The mol. wt was estimated to be 62,000 in non-reducing conditions and 64,500 in reducing conditions by SDS-PAGE. The isoelectric point was found to be pH 5.6. The enzyme had weak amidolytic activities toward CBS 65-25, but it showed no activities on S-2266, S-2302, thrombin substrate S-2238, plasmin substrate S-2251 or factor Xa substrate S-2222. It had no arginine esterase activity toward substrate benzoylarginine ethylester (BAEE). The enzyme activated factor X in vitro and the effect was absolutely Ca2+ dependent, with a Hill coefficient of 6.83. It could not activate prothrombin nor had any effect on fibrinogen and thus appeared to act specifically on factor X. The procoagulant activity of the enzyme was almost completely inhibited by serine protease inhibitors like PMSF, TPCK and soybean trypsin inhibitor; partially inhibited by L-cysteine. Metal chelator EDTA did not inhibit its procoagulant activity. These results suggest that the factor X activator from O. hannah venom is a serine protease.
    MeSH term(s) Animals ; Arginine/analogs & derivatives ; Arginine/metabolism ; Blood Coagulation Factors/drug effects ; Calcium/metabolism ; Chemical Fractionation ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Elapid Venoms/enzymology ; Elapidae ; Electrophoresis, Polyacrylamide Gel ; Factor X/drug effects ; Humans ; Hydrogen-Ion Concentration ; Isoelectric Focusing ; Molecular Weight ; Rabbits ; Serine Endopeptidases/isolation & purification ; Serine Endopeptidases/metabolism ; Serine Endopeptidases/pharmacology ; Serine Proteinase Inhibitors/pharmacology ; Substrate Specificity
    Chemical Substances Blood Coagulation Factors ; Elapid Venoms ; Serine Proteinase Inhibitors ; Factor X (9001-29-0) ; Arginine (94ZLA3W45F) ; benzoylarginine ethyl ester (971-21-1) ; Serine Endopeptidases (EC 3.4.21.-) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 1995-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/0041-0101(95)00077-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Effects of an acidic phospholipase A2 purified from Ophiophagus hannah (king cobra) venom on rat heart.

    Huang, M Z / Wang, Q C / Liu, G F

    Toxicon : official journal of the International Society on Toxinology

    1993  Volume 31, Issue 5, Page(s) 627–635

    Abstract: An acidic phospholipase A2 (OHV A-PLA2) purified from Ophiophagus hannah venom had a cardiotoxic ...

    Abstract An acidic phospholipase A2 (OHV A-PLA2) purified from Ophiophagus hannah venom had a cardiotoxic action on rat heart. In rats OHV A-PLA2 (2-4 mg/kg) caused ECG abnormalities including decreased heart rate, prolonged P-R interval, widened QRS complex and complete A-V block. When tested on isolated rat right atria, OHV A-PLA2 (10-20 micrograms/ml) produced a positive chronotropic effect. When tested on isolated rat left atria or papillary muscle preparations, OHV A-PLA2 (2.5-20 micrograms/ml) caused positive inotropic effect, followed by contracture. The positive inotropic effects could be abolished by high Ca2+ and enhanced by low Ca2+; both treatments accelerated contracture. The contracture could be inhibited in Mn2+ (5 mM)-containing medium and abolished by Ca(2+)-free bath solution containing 1 mM EDTA. The cardiotoxic action of OHV A-PLA2 was not influenced by verapamil, tetrodotoxin, propranolol, phentolamine, atropine or indomethacin. It is suggested that the cardiotoxic effects of OHV A-PLA2 may result from increasing intracellular levels of Ca2+.
    MeSH term(s) Anesthesia ; Animals ; Atrioventricular Node/drug effects ; Calcium/pharmacology ; Elapid Venoms/antagonists & inhibitors ; Elapid Venoms/enzymology ; Elapid Venoms/toxicity ; Electrocardiography/drug effects ; Female ; Heart/drug effects ; Heart Atria/drug effects ; Heart Rate/drug effects ; In Vitro Techniques ; Magnesium/pharmacology ; Male ; Manganese/pharmacology ; Myocardial Contraction/drug effects ; Papillary Muscles/drug effects ; Phospholipases A/antagonists & inhibitors ; Phospholipases A/isolation & purification ; Phospholipases A/toxicity ; Phospholipases A2 ; Rats ; Rats, Wistar
    Chemical Substances Elapid Venoms ; Manganese (42Z2K6ZL8P) ; Phospholipases A (EC 3.1.1.32) ; Phospholipases A2 (EC 3.1.1.4) ; Magnesium (I38ZP9992A) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 1993-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/0041-0101(93)90117-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Isolation and properties of L-amino acid oxidase from Ophiophagus hannah venom.

    Hu, R / Wang, J / Lei, K

    Scientia Sinica. Series B, Chemical, biological, agricultural, medical & earth sciences

    1982  Volume 25, Issue 9, Page(s) 941–952

    Abstract: ... hannah venom. The differences between L-amino acid oxidase from Ophiophagus hannah and ...

    Abstract This paper reports the isolation and some properties of L-amino acid oxidase from Ophiophagus hannah venom. The differences between L-amino acid oxidase from Ophiophagus hannah and that from other sources in specific activity, properties and the spectrum of isozymes are noticeable. The result of electrophoresis on polyacrylamide gel shows that this purified enzyme is homogenous. The molecular weight determined by gradient polyacrylamide gel slab (4--30%) is around 15 X 10(4) dalton. The molecular weight of the subunit determined by SDS gradient gel electrophoresis (4--30%) is around 7.3 X 10(4) dalton. Therefore, this enzyme is composed of two subunits. The absorption spectrum reveals that there are two FADs in each molecule. The optimum pH of enzymic reaction is around 8.7--9.0 when L-leucine is used as substrate. The inhibition of the products is noticeable when substrate concentration goes beyond 3mM. This enzyme is heat stable and its activity would not decrease obviously after heating at 55 degrees C for 40 min. A linear relationship between enzyme concentration and reaction rate was noticed when enzyme concentration was below 5.7 micrograms/ml.
    MeSH term(s) Amino Acid Oxidoreductases/isolation & purification ; Amino Acid Oxidoreductases/metabolism ; Amino Acids/analysis ; Animals ; Flavin-Adenine Dinucleotide/analysis ; Kinetics ; L-Amino Acid Oxidase ; Macromolecular Substances ; Molecular Weight ; Snake Venoms/isolation & purification ; Snakes ; Species Specificity
    Chemical Substances Amino Acids ; Macromolecular Substances ; Snake Venoms ; Flavin-Adenine Dinucleotide (146-14-5) ; Amino Acid Oxidoreductases (EC 1.4.-) ; L-Amino Acid Oxidase (EC 1.4.3.2)
    Language English
    Publishing date 1982-09
    Publishing country China
    Document type Comparative Study ; Journal Article
    ZDB-ID 406604-2
    ISSN 0253-5823
    ISSN 0253-5823
    Database MEDical Literature Analysis and Retrieval System OnLINE

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