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  • Title: Use of lectin affinity chromatography for the purification of collagenase from human polymorphonuclear leukocytes.
    Author: Callaway JE, Garcia JA, Hersh CL, Yeh RK, Gilmore-Hebert M.
    Journal: Biochemistry; 1986 Aug 26; 25(17):4757-62. PubMed ID: 3021203.
    Abstract:
    Polymorphonuclear leukocytes (PMNLs) store collagenase in an inactive form in secretory granules. The enzyme can be activated in vitro by limited proteolysis or by sulfhydryl-modifying agents such as N-ethylmaleimide (NEM). We have enriched NEM-activated collagenase 820-fold using granule isolation, gel filtration, and wheat germ agglutinin (WGA)-agarose chromatography. The use of WGA-agarose resulted in a 55-fold enrichment of collagenase in a single step with very little loss of activity. The chromatographic behavior of collagenase on other lectin matrices was explored and gave information about the type of complex asparagine-linked oligosaccharide found on collagenase isolated from PMNLs.
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