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Improved detection of terminal transferase (TdT): The use of detergents on glutaraldehyde-fixed non-dehydrated cells prevents denaturation and diffusion artifacts.

Leuk. Res. 10, 1041-1049 (1986)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
TdT as an intranuclear enzyme mainly of immature lymphoid cells is commonly determined immunologically using air-dried cell smears fixed with methanol. Both cell dehydration and alcohol fixation were found here to denature TdT and surface antigens. This could be prevented by using non-dehydrated cells bound electrostatically to poly-L-lysine-coated slides, fixed minimally with glutaraldehyde and rendered permeable to antibodies by the non-ionic detergent Brij 56. Crosslinking glutaraldehyde in addition prevented diffusion of TdT to extranuclear sites. By avoiding artifacts of denaturation and diffusion, a higher sensitivity in the detection of TdT was achieved despite considerably lower quantities of antibody.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Detergents; glutaraldehyde; immunocytochemistry; methanol; polylysine; sensitivity; terminal transferase
ISSN (print) / ISBN 0145-2126
e-ISSN 1873-5835
Quellenangaben Volume: 10, Issue: 8, Pages: 1041-1049 Article Number: , Supplement: ,
Publisher Elsevier
Non-patent literature Publications
Reviewing status Peer reviewed