ADENOSINE TRIPHOSPHATASE LOCATED ON UNSTIMULATED HUMAN SMALL LYMPHOCYTE CELL MEMBRANES

A. S. Coulson, V. H. Zeitman, R. B. Cohn, E. Dong, R. B. Griepp, E. B. Stinson, N. E. Shumway

Research output: Contribution to journalArticlepeer-review

Abstract

This study was undertaken to localize the enzyme sodium‐potassium dependent adenosine triphosphatase in unstimulated human small lymphocytes using the histochemical technique of McClurkin [1964]. The substrate adenosine 5' triphosphate is hydrolyzed by the ATPase resulting in a lead phosphate precipitate at the site of enzyme action, subsequently visualized as lead sulphide. The enzyme was demonstrated in three different patterns, and for each donor the pattern was constant both on all four of the test slides, and on different occasions. The patterns observed were: clusters of granules related to the cell membrane; positive staining localized to portions of the cell membrane, and, less commonly, the whole cell circumference. The significance of this distribution may relate to areas with large numbers of antigen recognition sites on the lymphocyte membrane.

Original languageEnglish
Pages (from-to)181-186
Number of pages6
JournalExperimental Physiology
Volume62
Issue number2
DOIs
StatePublished - 7 Apr 1977
Externally publishedYes

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