Literature DB >> 1869517

Expression of cDNA for batroxobin, a thrombin-like snake venom enzyme.

M Maeda1, S Satoh, S Suzuki, M Niwa, N Itoh, I Yamashina.   

Abstract

The cloned cDNA for batroxobin has been expressed in E. coli. Batroxobin could only be obtained as intracellular aggregates of fusion proteins, fused with a small peptide. To obtain the mature batroxobin, the recognition sequence for thrombin was inserted between the peptide and the mature batroxobin. This fusion protein accumulated in an insoluble form and could easily be purified. After site-specific cleavage of the fusion protein with thrombin, recombinant batroxobin was isolated by preparative electrophoresis. Batroxobin with enzymatic activity was obtained by the refolding of recombinant batroxobin.

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Year:  1991        PMID: 1869517     DOI: 10.1093/oxfordjournals.jbchem.a123432

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  2 in total

1.  Effectiveness of topical haemocoagulase as a haemostatic agent in children undergoing extraction of primary teeth: a split-mouth, randomised, double-blind, clinical trial.

Authors:  D F Swamy; E S Barretto; J S L Rodrigues
Journal:  Eur Arch Paediatr Dent       Date:  2019-03-21

2.  Exploring the Utility of Recombinant Snake Venom Serine Protease Toxins as Immunogens for Generating Experimental Snakebite Antivenoms.

Authors:  Nessrin Alomran; Patricia Blundell; Jaffer Alsolaiss; Edouard Crittenden; Stuart Ainsworth; Charlotte A Dawson; Rebecca J Edge; Steven R Hall; Robert A Harrison; Mark C Wilkinson; Stefanie K Menzies; Nicholas R Casewell
Journal:  Toxins (Basel)       Date:  2022-06-29       Impact factor: 5.075

  2 in total

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