{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,18]],"date-time":"2026-02-18T23:13:06Z","timestamp":1771456386319,"version":"3.50.1"},"reference-count":62,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2018,11,28]],"date-time":"2018-11-28T00:00:00Z","timestamp":1543363200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2011\/23236-4"],"award-info":[{"award-number":["2011\/23236-4"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2015\/26609-7"],"award-info":[{"award-number":["2015\/26609-7"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2016\/20641-9"],"award-info":[{"award-number":["2016\/20641-9"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","award":["PNPD"],"award-info":[{"award-number":["PNPD"]}],"id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["476932\/2012-2"],"award-info":[{"award-number":["476932\/2012-2"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Snake venom serine proteases (SVSPs) are enzymes that are capable of interfering in various parts of the blood coagulation cascade, which makes them interesting candidates for the development of new therapeutic drugs. Herein, we isolated and characterized Moojase, a potent coagulant enzyme from Bothrops moojeni snake venom. The toxin was isolated from the crude venom using a two-step chromatographic procedure. Moojase is a glycoprotein with N-linked glycans, molecular mass of 30.3 kDa and acidic character (pI 5.80\u20136.88). Sequencing of Moojase indicated that it is an isoform of Batroxobin. Moojase was able to clot platelet-poor plasma and fibrinogen solutions in a dose-dependent manner, indicating thrombin-like properties. Moojase also rapidly induced the proteolysis of the A\u03b1 chains of human fibrinogen, followed by the degradation of the B\u03b2 chains after extended periods of incubation, and these effects were inhibited by PMSF, SDS and DTT, but not by benzamidine or EDTA. RP-HPLC analysis of its fibrinogenolysis confirmed the main generation of fibrinopeptide A. Moojase also induced the fibrinolysis of fibrin clots formed in vitro, and the aggregation of washed platelets, as well as significant amidolytic activity on substrates for thrombin, plasma kallikrein, factor Xia, and factor XIIa. Furthermore, thermofluor analyses and the esterase activity of Moojase demonstrated its very high stability at different pH buffers and temperatures. Thus, studies such as this for Moojase should increase knowledge on SVSPs, allowing their bioprospection as valuable prototypes in the development of new drugs, or as biotechnological tools.<\/jats:p>","DOI":"10.3390\/toxins10120500","type":"journal-article","created":{"date-parts":[[2018,11,28]],"date-time":"2018-11-28T11:43:44Z","timestamp":1543405424000},"page":"500","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1453-3185","authenticated-orcid":false,"given":"Fernanda G.","family":"Amorim","sequence":"first","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia, Departamento de An\u00e1lises Cl\u00ednicas, Toxicol\u00f3gicas e Bromatol\u00f3gicas, Faculdade de Ci\u00eancias Farmac\u00eauticas de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-903, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8133-3266","authenticated-orcid":false,"given":"Danilo L.","family":"Menaldo","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia, Departamento de An\u00e1lises Cl\u00ednicas, Toxicol\u00f3gicas e Bromatol\u00f3gicas, Faculdade de Ci\u00eancias Farmac\u00eauticas de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-903, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sante E. I.","family":"Carone","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia, Departamento de An\u00e1lises Cl\u00ednicas, Toxicol\u00f3gicas e Bromatol\u00f3gicas, Faculdade de Ci\u00eancias Farmac\u00eauticas de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-903, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thiago A.","family":"Silva","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia, Departamento de An\u00e1lises Cl\u00ednicas, Toxicol\u00f3gicas e Bromatol\u00f3gicas, Faculdade de Ci\u00eancias Farmac\u00eauticas de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-903, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marco A.","family":"Sartim","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia, Departamento de An\u00e1lises Cl\u00ednicas, Toxicol\u00f3gicas e Bromatol\u00f3gicas, Faculdade de Ci\u00eancias Farmac\u00eauticas de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-903, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Edwin","family":"De Pauw","sequence":"additional","affiliation":[{"name":"Laboratory of Mass Spectrometry, Department of Chemistry, University of Li\u00e8ge, 4000 Li\u00e8ge, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8153-9590","authenticated-orcid":false,"given":"Loic","family":"Quinton","sequence":"additional","affiliation":[{"name":"Laboratory of Mass Spectrometry, Department of Chemistry, University of Li\u00e8ge, 4000 Li\u00e8ge, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3274-180X","authenticated-orcid":false,"given":"Suely V.","family":"Sampaio","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia, Departamento de An\u00e1lises Cl\u00ednicas, Toxicol\u00f3gicas e Bromatol\u00f3gicas, Faculdade de Ci\u00eancias Farmac\u00eauticas de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-903, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2018,11,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.toxicon.2017.10.025","article-title":"New findings from the first transcriptome of the Bothrops moojeni snake venom gland","volume":"140","author":"Amorim","year":"2017","journal-title":"Toxicon"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.toxicon.2016.03.002","article-title":"Expression and partial biochemical characterization of a recombinant serine protease from Bothrops pauloensis snake venom","volume":"115","author":"Isabel","year":"2016","journal-title":"Toxicon"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.toxicon.2005.02.020","article-title":"Snake venom serine proteinases: Sequence homology vs. substrate specificity, a paradox to be solved","volume":"45","author":"Serrano","year":"2005","journal-title":"Toxicon"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.toxicon.2016.01.055","article-title":"Biochemical and functional characterization of BmooSP, a new serine protease from Bothrops moojeni snake venom","volume":"111","author":"Mamede","year":"2016","journal-title":"Toxicon"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1080\/15569540600567321","article-title":"Current status of snake venom thrombin-like enzymes","volume":"25","author":"Castro","year":"2006","journal-title":"Toxin Rev."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1016\/j.biochi.2012.07.007","article-title":"Biochemical characterization and comparative analysis of two distinct serine proteases from Bothrops pirajai snake venom","volume":"94","author":"Menaldo","year":"2012","journal-title":"Biochimie"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1016\/j.intimp.2013.02.023","article-title":"Effects of two serine proteases from Bothrops pirajai snake venom on the complement system and the inflammatory response","volume":"15","author":"Menaldo","year":"2013","journal-title":"Int. Immunopharmacol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1007\/s00018-003-3325-z","article-title":"Snake venom thrombin-like enzymes: From reptilase to now","volume":"61","author":"Castro","year":"2004","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.toxicon.2008.07.014","article-title":"Amino acid sequence of a kinin-releasing enzyme, KR-E-1, from the venom of Agkistrodon caliginosus (Kankoku-mamushi)","volume":"52","author":"Oyama","year":"2008","journal-title":"Toxicon"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"10246","DOI":"10.1074\/jbc.270.17.10246","article-title":"A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning","volume":"270","author":"Zhang","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/S0014-5793(00)01803-2","article-title":"Interaction of viper venom serine peptidases with thrombin receptors on human platelets","volume":"477","author":"Santos","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"39309","DOI":"10.1074\/jbc.M508502200","article-title":"Thrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases: Crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator","volume":"280","author":"Murakami","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1046\/j.1365-2567.2002.01490.x","article-title":"Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase","volume":"107","author":"Yamamoto","year":"2002","journal-title":"Immunology"},{"key":"ref_14","first-page":"241","article-title":"Factor V activation and inactivation by venom proteases","volume":"31","author":"Rosing","year":"2001","journal-title":"Haemostasis"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1097\/00001721-200011020-00005","article-title":"The cleavage and inactivation of plasminogen activator inhibitor type 1 and alpha2-antiplasmin by reptilase, a thrombin-like venom enzyme","volume":"11","author":"Urano","year":"2000","journal-title":"Blood Coagul. Fibrinolysis"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1016\/j.biochi.2013.04.006","article-title":"Cotiarinase is a novel prothrombin activator from the venom of Bothrops cotiara","volume":"95","author":"Kitano","year":"2013","journal-title":"Biochimie"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.jprot.2017.05.024","article-title":"Serine protease isoforms in Gloydius intermedius venom: Full sequences, molecular phylogeny and evolutionary implications","volume":"164","author":"Yang","year":"2017","journal-title":"J. Proteom."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1659","DOI":"10.4155\/fmc.14.99","article-title":"Cone snail venomics: From novel biology to novel therapeutics","volume":"6","author":"Prashanth","year":"2014","journal-title":"Future Med. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Radis-Baptista, G. (2013). Serine proteases\u2014Cloning, Expression and Potential Applications. An Integrated View of the Molecular Recognition and Toxinology-From Analytical Procedures to Biomedical Applications, InTech.","DOI":"10.5772\/3429"},{"key":"ref_20","unstructured":"PentaPharm (2018, November 27). Haemocoagulase. Available online: https:\/\/www.pentapharm.com\/content.cfm?nav=21&content=40."},{"key":"ref_21","unstructured":"PentaPharm (2018, November 27). Defibrase. Available online: https:\/\/www.pentapharm.com\/content.cfm?nav=21&content=39."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2927","DOI":"10.2174\/138161207782023739","article-title":"Approaching the golden age of natural product pharmaceuticals from venom libraries: an overview of toxins and toxin-derivatives currently involved in therapeutic or diagnostic applications","volume":"13","author":"Fox","year":"2007","journal-title":"Curr. Pharm. Des."},{"key":"ref_23","unstructured":"PentaPharm (2018, November 27). Pefakit Reptilase Time. Available online: https:\/\/www.pentapharm.com\/content.cfm?nav=11&content=26."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.taap.2018.08.018","article-title":"BjSP, a novel serine protease from Bothrops jararaca snake venom that degrades fibrinogen without forming fibrin clots","volume":"357","author":"Carone","year":"2018","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.toxicon.2012.11.010","article-title":"Biochemical and biological characterization of two serine proteinases from Colombian Crotalus durissus cumanensis snake venom","volume":"63","author":"Rucavado","year":"2013","journal-title":"Toxicon"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.toxicon.2013.11.007","article-title":"VaSP1, catalytically active serine proteinase from Vipera ammodytes ammodytes venom with unconventional active site triad","volume":"77","author":"Brgles","year":"2014","journal-title":"Toxicon"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.toxicon.2012.09.003","article-title":"The long road of research on snake venom serine proteinases","volume":"62","author":"Serrano","year":"2013","journal-title":"Toxicon"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"7186","DOI":"10.1021\/bi00021a033","article-title":"Purification, characterization, and amino acid sequence of a serine proteinase, PA-BJ, with platelet-aggregating activity from the venom of Bothrops jararaca","volume":"34","author":"Serrano","year":"1995","journal-title":"Biochemistry"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1111\/j.1538-7836.2008.02995.x","article-title":"Bothrops protease A, a unique highly glycosylated serine proteinase, is a potent, specific fibrinogenolytic agent","volume":"6","author":"Prezoto","year":"2008","journal-title":"J. Thromb. Haemost."},{"key":"ref_30","first-page":"1069","article-title":"Purification and partial characterization of a new proteolytic enzyme from the venom of Bothrops moojeni (CAISSACA)","volume":"47","author":"Oliveira","year":"1999","journal-title":"Biochem. Mol. Biol. Int."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/0041-0101(93)90182-I","article-title":"Basic proteinases from Bothrops moojeni (caissaca) venom--I. Isolation and activity of two serine proteinases, MSP 1 and MSP 2, on synthetic substrates and on platelet aggregation","volume":"31","author":"Serrano","year":"1993","journal-title":"Toxicon"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.toxicon.2013.10.016","article-title":"Rapid purification of serine proteinases from Bothrops alternatus and Bothrops moojeni venoms","volume":"76","author":"Ullah","year":"2013","journal-title":"Toxicon"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1007\/BF01924816","article-title":"Biochemische studien \u00fcber die gifte der schlangengattung Bothrops","volume":"192","year":"1939","journal-title":"Naunyn-Schmiedebergs Arch. Exp. Pathol. Pharmakol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/j.bbamem.2014.10.037","article-title":"Phospholipases a2 from Viperidae snakes: Differences in membranotropic activity between enzymatically active toxin and its inactive isoforms","volume":"1848","author":"Ghazaryan","year":"2015","journal-title":"Biochim. Biophys. Acta (BBA)-Biomembr."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Mukherjee, A.K., Kalita, B., and Thakur, R. (2014). Two acidic, anticoagulant PLA2 isoenzymes purified from the venom of monocled cobra Naja kaouthia exhibit different potency to inhibit thrombin and factor Xa via phospholipids independent, non-enzymatic mechanism. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0101334"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1016\/S0041-0101(03)00076-X","article-title":"Resolution of isoforms of mutalysin II, the metalloproteinase from bushmaster snake venom","volume":"41","author":"Sanchez","year":"2003","journal-title":"Toxicon"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"6636","DOI":"10.1016\/S0021-9258(18)63454-4","article-title":"Microheterogeneity of l-amino acid oxidase separation of multiple components by polyacrylamide gel electrofocusing","volume":"244","author":"Hayes","year":"1969","journal-title":"J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1055\/s-0038-1651479","article-title":"The activation of plasma factor XIII with the snake venom enzymes ancrod and batroxobin marajoensis","volume":"38","author":"Walter","year":"1977","journal-title":"Thromb. Haemost."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1111\/j.1749-6632.2001.tb03507.x","article-title":"Fibrin formation and proteolysis during ancrod treatment. Evidence for des-A-profibrin formation and thrombin independent factor XIII activity","volume":"936","author":"Dempfle","year":"2001","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1007\/s11239-016-1343-6","article-title":"Ancrod revisited: Viscoelastic analyses of the effects of Calloselasma rhodostoma venom on plasma coagulation and fibrinolysis","volume":"42","author":"Nielsen","year":"2016","journal-title":"J. Thromb. Thrombolysis"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1016\/S0300-9084(00)01178-0","article-title":"Snake venom proteins acting on hemostasis","volume":"82","author":"Braud","year":"2000","journal-title":"Biochimie"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/S0167-4838(99)00268-X","article-title":"Snake venom proteases affecting hemostasis and thrombosis","volume":"1477","author":"Matsui","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1360","DOI":"10.1111\/j.1538-7836.2008.03057.x","article-title":"The cut of the clot(h): Snake venom fibrinogenases as therapeutic agents","volume":"6","author":"Gardiner","year":"2008","journal-title":"J. Thromb. Haemost."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1177\/108705710100600609","article-title":"High-density miniaturized thermal shift assays as a general strategy for drug discovery","volume":"6","author":"Pantoliano","year":"2001","journal-title":"J. Biomol. Screen"},{"key":"ref_45","first-page":"1864","article-title":"ThermoFMN-a thermofluor assay developed for ligand-screening as an alternative strategy for drug discovery","volume":"25","author":"Tomaleri","year":"2014","journal-title":"J. Braz. Chem. Soc."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.pep.2013.08.002","article-title":"Optimization of protein purification and characterization using Thermofluor screens","volume":"91","author":"Boivin","year":"2013","journal-title":"Protein Exp. Purif."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.toxicon.2016.12.007","article-title":"Structural and binding studies of a C-type galactose-binding lectin from Bothrops jararacussu snake venom","volume":"126","author":"Sartim","year":"2017","journal-title":"Toxicon"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.biortech.2011.11.059","article-title":"A novel and efficient method for the immobilization of thermolysin using sodium chloride salting-in and consecutive microwave irradiation","volume":"115","author":"Chen","year":"2012","journal-title":"Bioresour. Technol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1110\/ps.041009005","article-title":"Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli","volume":"14","author":"Balaji","year":"2005","journal-title":"Protein Sci."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"197","DOI":"10.4161\/pri.28938","article-title":"The therapeutic potential of chemical chaperones in protein folding diseases","volume":"8","author":"Cortez","year":"2014","journal-title":"Prion"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"13997","DOI":"10.1073\/pnas.0606236103","article-title":"A molecular mechanism for osmolyte-induced protein stability","volume":"103","author":"Street","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.bpc.2005.08.010","article-title":"Ion hydration: Implications for cellular function, polyelectrolytes, and protein crystallization","volume":"119","author":"Collins","year":"2006","journal-title":"Biophys. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"105476","DOI":"10.1039\/C6RA20975K","article-title":"The effect of spermidine on the structure, kinetics and stability of proteinase K: Spectroscopic and computational approaches","volume":"6","author":"Shareghi","year":"2016","journal-title":"RSC Adv."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1139\/y59-157","article-title":"A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin","volume":"37","author":"Hummel","year":"1959","journal-title":"Can. J. Biochem. Physiol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1111\/j.1432-1033.1967.tb00047.x","article-title":"A protein sequenator","volume":"1","author":"Edman","year":"1967","journal-title":"Eur. J. Biochem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"M111.010587","DOI":"10.1074\/mcp.M111.010587","article-title":"PEAKS DB: De novo sequencing assisted database search for sensitive and accurate peptide identification","volume":"11","author":"Zhang","year":"2012","journal-title":"Mol. Cell. Proteom."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1016\/j.bbagen.2012.07.011","article-title":"BJ-PI2, a non-hemorrhagic metalloproteinase from Bothrops jararaca snake venom","volume":"1820","author":"Lorenzetti","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/0049-3848(73)90082-0","article-title":"The proteolytic action of ancrod on human fibrinogen and its polypeptide chains","volume":"2","author":"Edgar","year":"1973","journal-title":"Thromb. Res."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/S1095-6433(99)00166-X","article-title":"Coagulation and fibrinolysis in capybara (Hydrochaeris hydrochaeris), a close relative of the guinea-pig (Cavia porcellus)","volume":"125","author":"Polizello","year":"2000","journal-title":"Comp. Biochem. Physiol. A Mol. Integr. Physiol."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Lopes-Pires, M.E., Naime, A.C., Almeida Cardelli, N.J., Anjos, D.J., Antunes, E., and Marcondes, S. (2015). PKC and AKT Modulate cGMP\/PKG Signaling Pathway on Platelet Aggregation in Experimental Sepsis. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0137901"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1038\/nprot.2007.321","article-title":"The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability","volume":"2","author":"Niesen","year":"2007","journal-title":"Nat. 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