References
1. Kuddus M, Ramteke PW. Recent developments in production and biotechnological applications of cold-active microbial proteases. Crit Rev Microbiol. 2012;38:330–8.PubMedCrossRef 2. Fein H, Maytin EV, Mutasim DF, Bailin PL. Topical protease therapy as a novel method of epidermal ablation: preliminary report. Dermatol Surg. 2005;31:139–47.PubMedCrossRef 3. Craik CS, Page MJ, Madison EL. Proteases as therapeutics. Biochem J. 2011;435:1–16.PubMedCrossRef 4. Duffy MJ, McGowan PM, Gallagher WM. Cancer invasion and metastasis: changing views. J Pathol. 2008;214:283–93.PubMedCrossRef 5. Scott CJ, Taggart CC. Biologic protease inhibitors as novel therapeutic agents. Biochimie. 2010;92:1681–8.PubMedCrossRef 6. Rawlings ND, Tolle DP, Barrett AJ. Evolutionary families of peptidase inhibitors. Biochem J. 2004;378:705–16.PubMedCrossRef 7. Morris RT. The action of trypsin, pancreatic extract MGCD0103 solubility dmso and pepsin upon sloughs, coagula, and mucopus. NY Med J. 1891;53:424–6. 8. Morani AD. Trypsin therapy in the management of chronic surface ulcers. Plast Reconstr Surg. 1953;11:372–9.CrossRef 9. Rapoport C. The
use of trypsin in the therapy of tuberculous lymphadenitis and tuberculous fistulae. Dis Chest. 1958;34:154–61.PubMedCrossRef 10. Gudmundsdottir A, Palsdottir HM. Atlantic cod trypsins: from basic research to practical https://www.selleckchem.com/products/p5091-p005091.html applications. Mar Biotechnol. 2005;7:77–88.PubMedCrossRef 11. Seiberg M, Siock P, Wisniewski S, Cauwenbergh G, Shapiro SS. The effects of trypsin Amylase on apoptosis, utriculi size, and skin elasticity in the Rhino mouse. J Investig Dermatol. 1997;109:370–6.PubMedCrossRef 12. Shi L, Carson D. Collagenase Santyl ointment: a selective agent for wound debridement. J Wound Ostomy Cont Nurs. 2009;36(Suppl.):S12–6.CrossRef 13. Hellgren L. Cleansing properties of stabilized trypsin and streptokinase-streptodornase in necrotic leg ulcers. Eur
J Clin Pharmacol. 1983;24:623–8.PubMedCrossRef 14. Brooks JL, Jefferson KK. Staphylococcal biofilms: quest for the magic bullet. Adv Appl Microbiol. 2012;81:63–87.PubMedCrossRef 15. Chaignon P, Sadovskaya I, Ragunah C, Ramasubbu N, Kaplan JB, Jabbouri S. Susceptibility of staphylococcal biofilms to enzymatic treatments depends on their chemical composition. Appl Microbiol Biotechnol. 2007;75:125–32.PubMedCrossRef 16. Marti M, Trotonda MP, Tormo-Mas MA, et al. Extracellular proteases inhibit protein-dependent biofilm Ganetespib nmr formation in Staphylococcus aureus. Microbes Infect. 2010;12:55–64.PubMedCrossRef 17. Hangler M, Burmolle M, Schneider I, Allermann K, Jensen B. The serine protease Esperase HPF inhibits the formation of multispecies biofilm. Biofouling. 2009;25:667–74.PubMedCrossRef 18. Siddiqui KS, Cavicchioli R. Cold-adapted enzymes. Ann Rev Biochem. 2006;75:403–33.PubMedCrossRef 19. Lonhienne T, Gerday C, Feller G. Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim Biophys Acta. 2000;1543:1–10.PubMedCrossRef 20.