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- W1994300369 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." @default.
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- W1994300369 date "1986-08-26" @default.
- W1994300369 modified "2023-09-25" @default.
- W1994300369 title "Use of lectin affinity chromatography for the purification of collagenase from human polymorphonuclear leukocytes" @default.
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- W1994300369 doi "https://doi.org/10.1021/bi00365a006" @default.
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