Year: 1981
Type: article
Abstract: Evidence was obtained regarding the way the O-2-forming NADPH oxidase of human neutrophils is arranged within the plasma membrane. O-2 production by particles from zymosan-activated human neutrophils rose two- to threefold when the particles were assayed in the presence of appropriate concentrations of Triton X-100. The portion of activity revealed by the detergent was not affected by treating the particles with trypsin or with p-chloromercuribenzene sulfonate, a nonpenetrating sulfhydryl reagent, but the activity detectable in the absence of detergent was abolished by these treatments. O-2 production by phagocytic vesicles was not augmented by detergent, and was almost entirely eliminated by tryptic digestion of the vesicles regardless of whether or not detergent was present during the assay. These results suggest that the O-2-forming oxidase is embedded in the plasma membrane with a portion extending into the cytoplasm and the rest buried in the lipid bilayer. It is proposed that the pyridine nucleotide-binding site is located on the cytoplasmic extension and the oxygen binding site is on the intramembranous portion of the enzyme.
DOI: 10.1172/jci110210
Institution: Tufts Medical Center
Language: English
Subfield: Immunology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1969356572