Five Sepharose-bound ligands for the chromatographic purification of Clostridium collagenase and clostripain - PubMed (original) (raw)

Five Sepharose-bound ligands for the chromatographic purification of Clostridium collagenase and clostripain

I Emöd et al. FEBS Lett. 1977.

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Consecutive use of omega-aminoalkylagaroses. Resolution and purification of clostripain and collagenase from Clostridium histolyticum.
Kula MR, Hatef-Haghi D, Tauber-Finkelstein M, Shaltiel S. Kula MR, et al. Biochem Biophys Res Commun. 1976 Mar 22;69(2):389-96. doi: 10.1016/0006-291x(76)90534-9. Biochem Biophys Res Commun. 1976. PMID: 178310 No abstract available.
Purification of procollagenase and collagenase by affinity chromatography on Sepharose-collagen.
Gillet C, Eeckhout Y, Vaes G. Gillet C, et al. FEBS Lett. 1977 Feb 15;74(1):126-8. doi: 10.1016/0014-5793(77)80768-0. FEBS Lett. 1977. PMID: 190039 No abstract available.
Isolation by affinity chromatography of neutral proteinase from Clostridium histolyticum.
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[Biospecific chromatography of proteases (review)].
Vesa VS. Vesa VS. Prikl Biokhim Mikrobiol. 1980 Sep-Oct;16(5):629-52. Prikl Biokhim Mikrobiol. 1980. PMID: 6252554 Review. Russian. No abstract available.
Separation of proteases: old and new approaches.
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Some newly characterized collagenases from procaryotes and lower eucaryotes.
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The lanthanide-enhanced affinity chromatography of clostridial collagenase.
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L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L.
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