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. 1997 Nov 3;139(3):613–623. doi: 10.1083/jcb.139.3.613

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Determination of the number of glycans required for calnexin or calreticulin binding. Consensus glycosylation sequences were deleted by increasing, in single increments, from the NH₂ to the COOH terminus (lanes 2–8), and from the COOH to the NH₂ terminus (lanes 9–15). ³⁵S-HA was translated in vitro for 1 h at 32°C, alkylated, lysed, and precipitated with anti-HA, -calnexin (CNX), or -calreticulin (CRT) antisera. The labeled HA was resolved by nonreducing (A, NR) and reducing (B–D, RD) SDS-PAGE and autoradiography. The band designated as UT corresponds to the untranslocated and unglycosylated HA.