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Ultrastructural localization of elastase-like enzymes in human neutrophils

JM Clark, BM Aiken, DW Vaughan and HM Kagan

The thiol ester, N-t-butyloxycarbonyl-L-alanine-p-nitrothiophenyl ester (Boc-Ala-SNp) has been synthesized and applied as an ultrastructural cytochemical substrate for leukocytic elastase-like enzymes. Incubation of fixed human neutrophils with Boc-Ala-SNp in the presence of gold ions generates electron-dense deposits of gold p-nitrothiophenolate in the nuclear membrane, endoplasmic reticulum, Golgi complex, mitochondria, and granules. Deposition of product is inhibited by pretreatment of cells with general and specific chemical inactivators of neutrophil elastase. This substrate appears to have significant potential as a probe for the ultrastructural localization of elastase- like activity.

Volume 28, Issue 1, pp. 90-92, 01/01/1980
Copyright © 1980 by The Histochemical Society


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The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 1980