| pubmed-article:3021203 | pubmed:abstractText | 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. | lld:pubmed |
