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The biosynthesis and processing of Leu-1, a human T lymphocyte antigen, has been studied with the use of a monoclonal antibody. This molecule exists on the cell surface as a 67,000 m.w. glycoprotein. Through a series of pulse-labeling studies, in conjunction with the use of the antibiotic tunicamycin and the enzyme Endo-H, the details of glycosylation, processing, and deposition at the cell membrane were examined. The protein backbone of the molecule is 58,000 m.w. High-mannose sugars are added to asparagine residues during synthesis. Within 20 min, these high mannose sugars are converted to complex type carbohydrates, including fucose. The fully processed glycoprotein appears at the cell surface within 30 min after synthesis. This sequence of events is similar to that for other cell surface glycoproteins, including HLA and vesicular stomatitus virus glycoprotein.
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