اخبار و اعلانات

 آمار

تعداد نشریات286
تعداد نشریات سازمان84
تعداد شماره‌ها2,996
تعداد مقالات33,553
تعداد مشاهده مقاله44,160,318
تعداد دریافت فایل اصل مقاله20,533,851
Nasri Nasrabadi, N, Vatanpour, H, Mohamadpour Dounighi, N, Najafi, M, Ahmadinejad, M, Bayatzadeh, M A. (1402). Biochemistry of the Thrombin-Like enzyme and Its Purification from Iranian Echis carinatus snake venom: its interaction with platelet receptors. سامانه مدیریت نشریات علمی, 78(6), 1822-1835. doi: 10.32592/ARI.2023.78.6.1822
N Nasri Nasrabadi; H Vatanpour; N Mohamadpour Dounighi; M Najafi; M Ahmadinejad; M A Bayatzadeh. "Biochemistry of the Thrombin-Like enzyme and Its Purification from Iranian Echis carinatus snake venom: its interaction with platelet receptors". سامانه مدیریت نشریات علمی, 78, 6, 1402, 1822-1835. doi: 10.32592/ARI.2023.78.6.1822
Nasri Nasrabadi, N, Vatanpour, H, Mohamadpour Dounighi, N, Najafi, M, Ahmadinejad, M, Bayatzadeh, M A. (1402). 'Biochemistry of the Thrombin-Like enzyme and Its Purification from Iranian Echis carinatus snake venom: its interaction with platelet receptors', سامانه مدیریت نشریات علمی, 78(6), pp. 1822-1835. doi: 10.32592/ARI.2023.78.6.1822
Nasri Nasrabadi, N, Vatanpour, H, Mohamadpour Dounighi, N, Najafi, M, Ahmadinejad, M, Bayatzadeh, M A. Biochemistry of the Thrombin-Like enzyme and Its Purification from Iranian Echis carinatus snake venom: its interaction with platelet receptors. سامانه مدیریت نشریات علمی, 1402; 78(6): 1822-1835. doi: 10.32592/ARI.2023.78.6.1822

Biochemistry of the Thrombin-Like enzyme and Its Purification from Iranian Echis carinatus snake venom: its interaction with platelet receptors

Archives of Razi Institute
مقاله 19، دوره 78، شماره 6، بهمن و اسفند 2023، صفحه 1822-1835    اصل مقاله (1.02 M)
نوع مقاله: Original Articles
شناسه دیجیتال (DOI): 10.32592/ARI.2023.78.6.1822
نویسندگان
N Nasri Nasrabadi1؛ H Vatanpour2؛ N Mohamadpour Dounighi* 3؛ M Najafi4؛ M Ahmadinejad5؛ M A Bayatzadeh3
1Student Research Committee, Pharmaceutical Sciences Research Centre, School of Pharmacy, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
2Department of Toxicology, School of Pharmacy, Shahid Beheshti University of Medical Sciences, Tehran, Iran
3Department of Venomous Animals and Anti-venom, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
4Department of Molecular Genetic and Animal Breeding, Gorgan University of Agricultural Sciences and Natural Resources, Golestan, Iran
5Blood Transfusion Research Center, Institute for Research and Education in Transfusion Medicine, Tehran, Iran
چکیده
Snake venoms are rich in valuable substances that have medical potential in the diagnosis and treatment of hemostatic diseases. The present paper was aimed at the purification and functional characterization basis of a thrombin-like enzyme and its role in the functioning of the coagulation cascade and platelet aggregation pathway. A thrombin-like serine protease was purified from the Iranian Echis carinatus venom (TLIECV), employing a one-step chromatographic procedure. This peptide was collected in high yield and purity by a single chromatographic step using RP-HPLC equipped with a C18 column. This peptide showed a 3000 Da molecular weight in gel-electrophoresis. Evidence in the SDS-PAGE gel has confirmed high recovery of fraction in optimal terms. Subsequently, this peptide was identified via its intact molecular mass and peptide mass fingerprint (PMF) using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS). Multiple sequence alignments were performed by ClustalW, the Bioedit software. Molegro Data Modeller (MDM) 3.0 software was used to predict the putative tertiary structure of the peptide. The enzyme possessed fibrinogenolytic, procoagulant, and aggregation inducer properties. Moreover, the SDS-PAGE (12%) was applied to examine fibrinogenolytic function. The purified enzyme degraded the Aα chain of fibrinogen while the Bβ and γ chains were not digested. According to that, the deficient human plasma in factor X and normal human plasma were also coagulated by TLIECV, it takes part in the common and intrinsic routes of the coagulation cascade. These findings proved that TLIECV is a serine protease identical to procoagulant thrombin-like snake venom proteases; however, it specifically releases the Aα chain of bovine fibrinogen. Because of its function to make up for the deficiency of factor X and its platelet aggregation inducer property, TLIECV could be considered a molecular impact to reveal the hemostasis mechanisms.
کلیدواژه‌ها
Blood coagulation؛ Platelet aggregation inducer؛ Platelet function؛ Snake venom؛ Thrombin-like
عنوان مقاله [English]
آنالیز بیوشیمیایی آنزیم شبه ترومبین و خالص سازی آن از زهر مارجعفری ایرانی Echis carinatus وبرهمکنش آن با گیرنده های پلاکتی
کلیدواژه‌ها [English]
انعقاد خون, عملکرد پلاکت, زهر مار, ترومبین لایک, القا کننده تجمع پلاکتی
سایر فایل های مرتبط با مقاله
مراجع
References
1. Kadi-Saci A, Laraba-Djebari F. Purification and
characterization of a thrombin-like enzyme isolated
from Vipera lebetina venom: its interaction with platelet
receptor. Blood coagulation & fibrinolysis : an
international journal in haemostasis and thrombosis.
2020;31(1):1-10.
2. Damotharan P, Veeruraj A, Arumugam M,
Balasubramanian T. Isolation and characterization of
biologically active venom protein from sea snake
Enhydrina schistosa. Journal of biochemical and
molecular toxicology. 2015;29(3):140-7.
3. Castro HC, Zingali RB, Albuquerque MG, Pujol-Luz
M, Rodrigues CR. Snake venom thrombin-like
enzymes: from reptilase to now. Cellular and molecular
life sciences : CMLS. 2004;61(7-8):843-56.
4. Ullah A, Masood R, Ali I, Ullah K, Ali H, Akbar H, et
al. Thrombin-like enzymes from snake venom:
Structural characterization and mechanism of action.
International journal of biological macromolecules.
2018;114:788-811.
5. Bell WR, Jr. Defibrinogenating enzymes. Drugs.
1997;54 Suppl 3:18-30; discussion -1.
6. Au LC, Lin SB, Chou JS, Teh GW, Chang KJ, Shih
CM. Molecular cloning and sequence analysis of the
cDNA for ancrod, a thrombin-like enzyme from the
venom of Calloselasma rhodostoma. The Biochemical
journal. 1993;294 ( Pt 2)(Pt 2):387-90.
7. Burkhart W, Smith GF, Su JL, Parikh I, LeVine H, 3rd.
Amino acid sequence determination of ancrod, the
thrombin-like alpha-fibrinogenase from the venom of
Akistrodon rhodostoma. FEBS letters. 1992;297(3):
297-301.
8. Stocker K, Barlow GH. The coagulant enzyme from
Bothrops atrox venom (batroxobin). Methods in
enzymology. 1976;45:214-23.
9. Oyama E, Takahashi H. Purification and
characterization of a thrombin like enzyme, elegaxobin
II, with lys-bradykinin releasing activity from the
venom of Trimeresurus elegans (Sakishima-Habu).
Toxicon : official journal of the International Society on
Toxinology. 2003;41(5):559-68.
10. Alvarado J, Gutiérrez JM. Anticoagulant effect of
myotoxic phospholipase A2 isolated from the venom of
the snake Bothrops asper (Viperidae). Revista de
biologia tropical. 1988;36(2b):563-5.
11. Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M.
In-gel digestion for mass spectrometric characterization
of proteins and proteomes. Nature protocols.
2006;1(6):2856-60.
12. Shevchenko A, Tomas H, Havli J, Olsen JV, Mann M.
In-gel digestion for mass spectrometric characterization
of proteins and proteomes. Nature Protocols.
Nasri Nasrabadi N et al / Archives of Razi Institute, Vol. 78, No. 6 (2023) 1822-1835 1835
2006;1(6):2856-60.
13. Laraba-Djebari F, Martin-Eauclaire MF, Mauco G,
Marchot P. Afaâcytin, an alpha beta-fibrinogenase from
Cerastes cerastes (horned viper) venom, activates
purified factor X and induces serotonin release from
human blood platelets. European journal of
biochemistry. 1995;233(3):756-65.
14. Zaqueo KD, Kayano AM, Domingos TF, Moura LA,
Fuly AL, da Silva SL, et al. BbrzSP-32, the first serine
protease isolated from Bothrops brazili venom:
Purification and characterization. Comparative
biochemistry and physiology Part A, Molecular &
integrative physiology. 2016;195:15-25.
15. Silva-Junior FP, Guedes HL, Garvey LC, Aguiar AS,
Bourguignon SC, Di Cera E, et al. BJ-48, a novel
thrombin-like enzyme from the Bothrops jararacussu
venom with high selectivity for Arg over Lys in P1:
Role of N-glycosylation in thermostability and active
site accessibility. Toxicon : official journal of the
International Society on Toxinology. 2007;50(1):18-31.
16. Sant' Ana CD, Ticli FK, Oliveira LL, Giglio JR, Rechia
CGV, Fuly AL, et al. BjussuSP-I: a new thrombin-like
enzyme isolated from Bothrops jararacussu snake
venom. Comparative biochemistry and physiology Part
A, Molecular & integrative physiology. 2008;
151(3):443-54.
17.Boldrini-França J, Pinheiro-Junior EL, Arantes EC.
Functional and biological insights of rCollinein-1, a
recombinant serine protease from Crotalus durissus
collilineatus. The journal of venomous animals and
toxins including tropical diseases. 2019;25:e147118.
18. Oyama E, Takahashi H. Amino acid sequence of a
thrombin like enzyme, elegaxobin, from the venom of
Trimeresurus elegans (Sakishima-habu). Toxicon :
official journal of the International Society on
Toxinology. 2002;40(7):959-70.
19. Oyama E, Takahashi H. Substrate specificity of two
thrombin like enzymes (elegaxobin, elegaxobin II) from
the venom of Trimeresurus elegans (Sakishima-habu),
using neutralizing antibody. Toxicon : official journal of
the International Society on Toxinology. 2006;48(6):
601-10.
20. Tan NH. Isolation and characterization of the thrombinlike enzyme from Cryptelytrops purpureomaculatus
venom. Comparative biochemistry and physiology
Toxicology & pharmacology : CBP. 2010;151(1):131-6.
21. Shieh TC, Kawabata S, Kihara H, Ohno M, Iwanaga S.
Amino acid sequence of a coagulant enzyme,
flavoxobin, from Trimeresurus flavoviridis venom.
Journal of biochemistry. 1988;103(4):596-605.
22. Oyama E, Takahashi H. Purification and
characterization of a thrombin-like enzyme, elegaxobin,
from the venom of Trimeresurus elegans (Sakishimahabu). Toxicon : official journal of the International
Society on Toxinology. 2000;38(8):1087-100.
23. Pirkle H, Theodor I, Lopez R. Catroxobin, a weakly
thrombin-like enzyme from the venom of Crotalus
atrox. NH2-terminal and active site amino acid
sequences. Thrombosis research. 1989;56(2):159-68.
24. Pirkle H, Markland FS, Theodor I, Baumgartner R,
Bajwa SS, Kirakossian H. The primary structure of
crotalase, a thrombin-like venom enzyme, exhibits
closer homology to kallikrein than to other serine
proteases. Biochemical and biophysical research
communications. 1981;99(2):715-21.
25. Pirkle H, Theodor I, Miyada D, Simmons G. Thrombinlike enzyme from the venom of Bitis gabonica.
Purification, properties, and coagulant actions. The
Journal of biological chemistry. 1986;261(19):8830-5.
26.Banfield DK, Irwin DM, Walz DA, MacGillivray RTA.
Evolution of prothrombin: Isolation and characterization
of the cDNAs encoding chicken and hagfish
prothrombin. Journal of Molecular Evolution. 1994;
38(2):177-87.
27. Swift GH, Dagorn JC, Ashley PL, Cummings SW,
MacDonald RJ. Rat pancreatic kallikrein mRNA:
nucleotide sequence and amino acid sequence of the
encoded preproenzyme. Proceedings of the National
Academy of Sciences of the United States of America.
1982;79(23):7263-7.
28. Titani K, Ericsson LH, Neurath H, Walsh KA. Amino
acid sequence of dogfish trypsin. Biochemistry.
1975;14(7):1358-66.

آمار
تعداد مشاهده مقاله: 17,542
تعداد دریافت فایل اصل مقاله: 483


counter
سامانه مدیریت نشریات علمی. طراحی و پیاده سازی از سیناوب