{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,8,9]],"date-time":"2024-08-09T21:10:49Z","timestamp":1723237849849},"reference-count":39,"publisher":"Walter de Gruyter GmbH","issue":"4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019,3,26]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec id=\"j_cclm-2018-0397_s_999_w2aab3b7c35b1b6b1aab1c16b1Aa\">\n                  <jats:title>Background<\/jats:title>\n                  <jats:p>Incomplete blood clotting or latent clotting in serum is a common laboratory problem, especially for patients on anticoagulant therapy or when serum tubes are centrifuged before clotting is completed. We describe a novel approach to producing high-quality serum using snake venom prothrombin activator complex (OsPA) as an additive in blood collection tubes for non-anticoagulated (normal) individuals.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec id=\"j_cclm-2018-0397_s_998_w2aab3b7c35b1b6b1aab1c16b2Aa\">\n                  <jats:title>Methods<\/jats:title>\n                  <jats:p>Plasma clotting assays were performed using a Hyland-Clotek instrument. Blood clotting was visually observed, and thromboelastography was also performed to determine the important parameters of coagulation. Thrombin generation was assayed using the chromogenic substrate S-2238, and biochemical analytes in the serum were determined on chemistry and immunoassay analysers. Fibrinogen was determined by either ELISA or Clauss fibrinogen assay.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec id=\"j_cclm-2018-0397_s_997_w2aab3b7c35b1b6b1aab1c16b3Aa\">\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>We initially showed that OsPA had strong coagulation activity in clotting not only recalcified citrated plasma and recalcified citrated whole blood, but also fresh whole blood in a clinical setting. The use of TEG clearly showed improved speed of clotting and generation of a firmer clot. We also showed that the use of OsPA to produce serum did not interfere with the determination of commonly measured biochemical analytes. The underlying clotting mechanism involves a burst of thrombin production at the initial stages of the clotting process upon contact with prothrombin in blood.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec id=\"j_cclm-2018-0397_s_996_w2aab3b7c35b1b6b1aab1c16b4Aa\">\n                  <jats:title>Conclusions<\/jats:title>\n                  <jats:p>These results demonstrate rapid generation of high-quality serum, contributing to faster turnaround times with standardised quality samples, for accurate analyte determinations in normal individuals.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1515\/cclm-2018-0397","type":"journal-article","created":{"date-parts":[[2018,9,29]],"date-time":"2018-09-29T09:01:15Z","timestamp":1538211675000},"page":"483-497","source":"Crossref","is-referenced-by-count":6,"title":["Next-generation rapid serum tube technology using prothrombin activator coagulant: fast, high-quality serum from normal samples"],"prefix":"10.1515","volume":"57","author":[{"given":"Kong-Nan","family":"Zhao","sequence":"first","affiliation":[{"name":"Centre for Venomics Research, School of Medicine , The University of Queensland, Translational Research Institute , Woolloongabba, QLD , Australia"},{"name":"Centre for Clinical Research, The University of Queensland, Royal Brisbane and Women\u2019s Hospital Campus , Herston, Brisbane, QLD , Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Goce","family":"Dimeski","sequence":"additional","affiliation":[{"name":"Chemical Pathology, Princess Alexandra Hospital , Woolloongabba, Brisbane, QLD , Australia"},{"name":"School of Chemistry and Molecular Biosciences , The University of Queensland, Brisbane , QLD , Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John","family":"de Jersey","sequence":"additional","affiliation":[{"name":"School of Chemistry and Molecular Biosciences , The University of Queensland, Brisbane , QLD , Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lambro A.","family":"Johnson","sequence":"additional","affiliation":[{"name":"Centre for Venomics Research, School of Medicine , The University of Queensland, Translational Research Institute , Woolloongabba, QLD , Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Grant","sequence":"additional","affiliation":[{"name":"Q-Sera Pty Ltd , Melbourne, VIC , Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul P.","family":"Masci","sequence":"additional","affiliation":[{"name":"Centre for Venomics Research, School of Medicine , The University of Queensland, Translational Research Institute , Woolloongabba, QLD , Australia"},{"name":"Centre for Clinical Research, The University of Queensland, Royal Brisbane and Women\u2019s Hospital Campus , Herston, Brisbane, QLD , Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martin F.","family":"Lavin","sequence":"additional","affiliation":[{"name":"Centre for Clinical Research, The University of Queensland, Royal Brisbane and Women\u2019s Hospital Campus , Herston, Brisbane, QLD 4029 , Australia , Phone: +61 07 3346 6045, Fax: +61 07 3346 5509"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"374","published-online":{"date-parts":[[2018,9,29]]},"reference":[{"key":"2021021219385196173_j_cclm-2018-0397_ref_001_w2aab3b7c35b1b6b1ab2b2b1Aa","doi-asserted-by":"crossref","unstructured":"Vignati G, Chiecchio A, Osnaghi B, Giovanelli L, Meloncelli C. Different biological matrices (serum and plasma) utilization in consolidation processes: evaluation of seven access immunoassays. Clin Chem Lab Med 2008;46:264\u201370.","DOI":"10.1515\/CCLM.2008.032"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_002_w2aab3b7c35b1b6b1ab2b2b2Aa","doi-asserted-by":"crossref","unstructured":"Lee BS, Lee YU, Kim HS, Kim TH, Park J, Lee JG, et al. Fully integrated lab-on-a-disc for simultaneous analysis of biochemistry and immunoassay from whole blood. Lab Chip 2011;11:70\u20138.","DOI":"10.1039\/C0LC00205D"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_003_w2aab3b7c35b1b6b1ab2b2b3Aa","doi-asserted-by":"crossref","unstructured":"Bowen RA, Sattayapiwat A, Gounden V, Remaley AT. Blood collection tube-related alterations in analyte concentrations in quality control material and serum specimens. Clin Biochem 2014;47:150\u20137.","DOI":"10.1016\/j.clinbiochem.2013.11.003"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_004_w2aab3b7c35b1b6b1ab2b2b4Aa","doi-asserted-by":"crossref","unstructured":"Aoki N, Sakata Y, Ichinose A. Fibrin-associated plasminogen activation in alpha 2-plasmin inhibitor deficiency. Blood 1983;62:1118\u201322.","DOI":"10.1182\/blood.V62.5.1118.1118"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_005_w2aab3b7c35b1b6b1ab2b2b5Aa","doi-asserted-by":"crossref","unstructured":"Cuhadar S, Atay A, Koseoglu M, Dirican A, Hur A. Stability studies of common biochemical analytes in serum separator tubes with or without gel barrier subjected to various storage conditions. Biochem Med (Zagreb) 2012;22:202\u201314.","DOI":"10.11613\/BM.2012.023"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_006_w2aab3b7c35b1b6b1ab2b2b6Aa","doi-asserted-by":"crossref","unstructured":"Dimeski G, Masci PP, Trabi M, Lavin MF, De Jersey J. Evaluation of the Becton-Dickinson rapid serum tube: does it provide a suitable alternative to lithium heparin plasma tubes? Clin Chem Lab Med 2010;48:651\u20137.","DOI":"10.1515\/CCLM.2010.141"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_007_w2aab3b7c35b1b6b1ab2b2b7Aa","doi-asserted-by":"crossref","unstructured":"Dimeski G, Solano C, Petroff MK, Hynd M. Centrifugation protocols: tests to determine optimal lithium heparin and citrate plasma sample quality. Ann Clin Biochem 2011;48:218\u201322.","DOI":"10.1258\/acb.2010.010230"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_008_w2aab3b7c35b1b6b1ab2b2b8Aa","unstructured":"Bowen RA, Remaley AT. Interferences from blood collection tube components on clinical chemistry assays. Biochem Med (Zagreb) 2014;24:31\u201344."},{"key":"2021021219385196173_j_cclm-2018-0397_ref_009_w2aab3b7c35b1b6b1ab2b2b9Aa","doi-asserted-by":"crossref","unstructured":"Prusa R, Doupovcova J, Warunek D, Stankovic AK. Improving laboratory efficiencies through significant time reduction in the preanalytical phase. Clin Chem Lab Med 2010;48:293\u20136.","DOI":"10.1515\/CCLM.2010.036"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_010_w2aab3b7c35b1b6b1ab2b2c10Aa","doi-asserted-by":"crossref","unstructured":"Dimeski G, Johnston J, Masci PP, Zhao KN, Brown N. Evaluation of the Greiner Bio-One serum separator BCA fast clot tube. Clin Chem Lab Med 2017;55:1135\u201341.","DOI":"10.1515\/cclm-2016-0806"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_011_w2aab3b7c35b1b6b1ab2b2c11Aa","doi-asserted-by":"crossref","unstructured":"Bompiani KM, Lohrmann JL, Pitoc GA, Frederiksen JW, Mackensen GB, Sullenger BA. Probing the coagulation pathway with aptamers identifies combinations that synergistically inhibit blood clot formation. Chem Biol 2014;21:935\u201344.","DOI":"10.1016\/j.chembiol.2014.05.016"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_012_w2aab3b7c35b1b6b1ab2b2c12Aa","doi-asserted-by":"crossref","unstructured":"Brummel-Ziedins K, Undas A, Orfeo T, Gissel M, Butenas S, Zmudka K, et al. Thrombin generation in acute coronary syndrome and stable coronary artery disease: dependence on plasma factor composition. J Thromb Haemost 2008;6:104\u201310.","DOI":"10.1111\/j.1538-7836.2007.02799.x"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_013_w2aab3b7c35b1b6b1ab2b2c13Aa","doi-asserted-by":"crossref","unstructured":"Ruggeri ZM, Ruggeri ZM. Platelet and von Willebrand factor interactions at the vessel wall. Hamostaseologie 2004;24:1\u201311.","DOI":"10.1055\/s-0037-1619601"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_014_w2aab3b7c35b1b6b1ab2b2c14Aa","doi-asserted-by":"crossref","unstructured":"Undas A, Szuldrzynski K, Brummel-Ziedins KE, Tracz W, Zmudka K, Mann KG. Systemic blood coagulation activation in acute coronary syndromes. Blood 2009;113:2070\u20138.","DOI":"10.1182\/blood-2008-07-167411"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_015_w2aab3b7c35b1b6b1ab2b2c15Aa","doi-asserted-by":"crossref","unstructured":"Stubbs MT, Bode W. Coagulation factors and their inhibitors. Curr Opin Struct Biol 1994;4:823\u201332.","DOI":"10.1016\/0959-440X(94)90263-1"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_016_w2aab3b7c35b1b6b1ab2b2c16Aa","doi-asserted-by":"crossref","unstructured":"Matafonov A, Sarilla S, Sun MF, Sheehan JP, Serebrov V, Verhamme IM, et al. Activation of factor Xi by products of prothrombin activation. Blood 2011;118:437\u201345.","DOI":"10.1182\/blood-2010-10-312983"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_017_w2aab3b7c35b1b6b1ab2b2c17Aa","doi-asserted-by":"crossref","unstructured":"Walker FJ, Owen WG, Esmon CT. Characterization of the prothrombin activator from the venom of Oxyuranus scutellatus scutellatus (Taipan Venom). Biochemistry 1980;19:1020\u20133.","DOI":"10.1021\/bi00546a029"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_018_w2aab3b7c35b1b6b1ab2b2c18Aa","doi-asserted-by":"crossref","unstructured":"Kini RM. The intriguing world of prothrombin activators from snake venom. Toxicon 2005;45:1133\u201345.","DOI":"10.1016\/j.toxicon.2005.02.019"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_019_w2aab3b7c35b1b6b1ab2b2c19Aa","doi-asserted-by":"crossref","unstructured":"Speijer H, Govers-Riemslag JW, Zwaal RF, Rosing J. Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan Snake). J Biol Chem 1986;261:13258\u201367.","DOI":"10.1016\/S0021-9258(18)69299-3"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_020_w2aab3b7c35b1b6b1ab2b2c20Aa","doi-asserted-by":"crossref","unstructured":"Speijer H, Govers-Riemslag JW, Zwaal RF, Rosing J. Platelet procoagulant properties studied with snake venom prothrombin activators. Thromb Haemost 1987;57:349\u201355.","DOI":"10.1055\/s-0038-1651132"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_021_w2aab3b7c35b1b6b1ab2b2c21Aa","doi-asserted-by":"crossref","unstructured":"Bos MH, Camire RM. Procoagulant adaptation of a blood coagulation prothrombinase-like enzyme complex in Australian elapid venom. Toxins (Basel) 2010;2:1554\u201367.","DOI":"10.3390\/toxins2061554"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_022_w2aab3b7c35b1b6b1ab2b2c22Aa","unstructured":"Bos MH, Camire RM. Blood coagulation factors V and VIII: molecular mechanisms of procofactor activation. J Coagul Disord 2010;2:19\u201327."},{"key":"2021021219385196173_j_cclm-2018-0397_ref_023_w2aab3b7c35b1b6b1ab2b2c23Aa","unstructured":"Austen DE, Rhymes IL. Laboratory Manual of Blood Coagulation. Oxford: Blackwell Scientific Publications, 1975:109."},{"key":"2021021219385196173_j_cclm-2018-0397_ref_024_w2aab3b7c35b1b6b1ab2b2c24Aa","doi-asserted-by":"crossref","unstructured":"Swallow RA, Agarwala RA, Dawkins KD, Curzen NP. Thromboelastography: potential bedside tool to assess the effects of antiplatelet therapy? Platelets 2006;17:385\u201392.","DOI":"10.1080\/09537100600757521"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_025_w2aab3b7c35b1b6b1ab2b2c25Aa","unstructured":"Masci PP, Whitaker AN, De Jersey J. Purification and characterization of a prothrombin activator from the venom of the Australian brown snake, Pseudonaja textilis textilis. Biochem Int 1988;17:825\u201335."},{"key":"2021021219385196173_j_cclm-2018-0397_ref_026_w2aab3b7c35b1b6b1ab2b2c26Aa","doi-asserted-by":"crossref","unstructured":"Moore GW, Tugnait S, Savidge GF. A new-generation dilute Russell\u2019s viper venom time assay system for lupus anticoagulants: evaluation of detection utilising frozen reagents and controls. Br J Biomed Sci 2005;62:127\u201332.","DOI":"10.1080\/09674845.2005.11732699"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_027_w2aab3b7c35b1b6b1ab2b2c27Aa","doi-asserted-by":"crossref","unstructured":"Nowak G. The Ecarin clotting time, a universal method to quantify direct thrombin inhibitors. Pathophysiol Haemost Thromb 2003;33:173\u201383.","DOI":"10.1159\/000081505"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_028_w2aab3b7c35b1b6b1ab2b2c28Aa","doi-asserted-by":"crossref","unstructured":"Van Cott EM, Smith EY, Galanakis DK. Elevated fibrinogen in an acute phase reaction prolongs the reptilase time but typically not the thrombin time. Am J Clin Pathol 2002;118: 263\u20138.","DOI":"10.1309\/WUB3-72JT-E50M-EU8J"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_029_w2aab3b7c35b1b6b1ab2b2c29Aa","doi-asserted-by":"crossref","unstructured":"Herrera M, Paiva OK, Pagotto AH, Segura A, Serrano SM, Vargas M, et al. Antivenomic characterization of two antivenoms against the venom of the Taipan, Oxyuranus scutellatus, from Papua New Guinea and Australia. Am J Trop Med Hyg 2014;91:887\u201394.","DOI":"10.4269\/ajtmh.14-0333"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_030_w2aab3b7c35b1b6b1ab2b2c30Aa","doi-asserted-by":"crossref","unstructured":"Arslan FD, Karakoyun I, Basok BI, Aksit MZ, Baysoy A, Ozturk YK, et al. The local clinical validation of a new lithium heparin tube with a barrier: Bd Vacutainer(R) Barricor Lh Plasma tube. Biochem Med (Zagreb) 2017;27:030706.","DOI":"10.11613\/BM.2017.030706"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_031_w2aab3b7c35b1b6b1ab2b2c31Aa","doi-asserted-by":"crossref","unstructured":"Carraro P, Servidio G, Plebani M. Hemolyzed specimens: a reason for rejection or a clinical challenge? Clin Chem 2000;46:306\u20137.","DOI":"10.1093\/clinchem\/46.2.306"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_032_w2aab3b7c35b1b6b1ab2b2c32Aa","doi-asserted-by":"crossref","unstructured":"Lippi G, Cervellin G, Mattiuzzi C. Critical review and meta-analysis of spurious hemolysis in blood samples collected from intravenous catheters. Biochem Med (Zagreb) 2013;23:193\u2013200.","DOI":"10.11613\/BM.2013.022"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_033_w2aab3b7c35b1b6b1ab2b2c33Aa","doi-asserted-by":"crossref","unstructured":"Monneret D, Mestari F, Atlan G, Corlouer C, Ramani Z, Jaffre J, et al. Hemolysis indexes for biochemical tests and immunoassays on roche analyzers: determination of allowable interference limits according to different calculation methods. Scand J Clin Lab Invest 2015;75:162\u20139.","DOI":"10.3109\/00365513.2014.993691"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_034_w2aab3b7c35b1b6b1ab2b2c34Aa","doi-asserted-by":"crossref","unstructured":"Rao VS, Kini RM. Pseutarin C, a prothrombin activator from Pseudonaja textilis venom: its structural and functional similarity to mammalian coagulation factor Xa-Va complex. Thromb Haemost 2002;88:611\u20139.","DOI":"10.1055\/s-0037-1613264"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_035_w2aab3b7c35b1b6b1ab2b2c35Aa","doi-asserted-by":"crossref","unstructured":"St Pierre L, Masci PP, Filippovich I, Sorokina N, Marsh N, Miller DJ, et al. Comparative analysis of prothrombin activators from the venom of Australian Elapids. Mol Biol Evol 2005;22:1853\u201364.","DOI":"10.1093\/molbev\/msi181"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_036_w2aab3b7c35b1b6b1ab2b2c36Aa","doi-asserted-by":"crossref","unstructured":"Bos MH, Boltz M, St Pierre L, Masci PP, De Jersey J, Lavin MF, et al. Venom Factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations. Blood 2009;114:686\u201392.","DOI":"10.1182\/blood-2009-02-202663"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_037_w2aab3b7c35b1b6b1ab2b2c37Aa","doi-asserted-by":"crossref","unstructured":"Plebani M, Lippi G. Improving diagnosis and reducing diagnostic errors: the next frontier of laboratory medicine. Clin Chem Lab Med 2016;54:1117\u20138.","DOI":"10.1515\/cclm-2016-0217"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_038_w2aab3b7c35b1b6b1ab2b2c38Aa","doi-asserted-by":"crossref","unstructured":"Lippi G, Plebani M, Favaloro EJ. The model list of essential in vitro diagnostics: nuisance or opportunity? Diagnosis (Berl) 2018. pii: \/j\/dx.ahead-of-print\/dx-2018-0035\/dx-2018-0035.xml. Doi: 10.1515\/dx-2018-0035. [Epub ahead of print].","DOI":"10.1515\/dx-2018-0035"},{"key":"2021021219385196173_j_cclm-2018-0397_ref_039_w2aab3b7c35b1b6b1ab2b2c39Aa","doi-asserted-by":"crossref","unstructured":"Plebani M, Lippi G. Improving the post-analytical phase. Clin Chem Lab Med 2010;48:435\u20136.","DOI":"10.1515\/CCLM.2010.113"}],"container-title":["Clinical Chemistry and Laboratory Medicine (CCLM)"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.degruyter.com\/view\/j\/cclm.2019.57.issue-4\/cclm-2018-0397\/cclm-2018-0397.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/cclm-2018-0397\/xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/cclm-2018-0397\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,4,21]],"date-time":"2021-04-21T22:40:38Z","timestamp":1619044838000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/cclm-2018-0397\/html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,9,29]]},"references-count":39,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2018,9,29]]},"published-print":{"date-parts":[[2019,3,26]]}},"alternative-id":["10.1515\/cclm-2018-0397"],"URL":"https:\/\/doi.org\/10.1515\/cclm-2018-0397","relation":{},"ISSN":["1437-4331","1434-6621"],"issn-type":[{"value":"1437-4331","type":"electronic"},{"value":"1434-6621","type":"print"}],"subject":[],"published":{"date-parts":[[2018,9,29]]}}}