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. 1996 Dec 1;184(6):2251–2260. doi: 10.1084/jem.184.6.2251

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Breakdown of unfolded K^b heavy chains at the cell surface. (A) RMA cells were starved for 45 min in the absence or presence of the vacuolar H⁺-ATPase inhibitor Con B, pulse-labeled for 5 min, and then chased for the times indicated. Class I heavy chains were directly immunoprecipitated from NP-40 detergent lysates (no initial preclear) with the antibodies indicated in each panel, and reimmunoprecipitated with the p8 antiserum before SDS–PAGE. (B) Phosphoimager quantitation of the band densities in A. The data sets for each pulse–chase were normalized around the 60 min chase point densities.

Breakdown of unfolded K^b heavy chains at the cell surface. (A) RMA cells were starved for 45 min in the absence or presence of the vacuolar H⁺-ATPase inhibitor Con B, pulse-labeled for 5 min, and then chased for the times indicated. Class I heavy chains were directly immunoprecipitated from NP-40 detergent lysates (no initial preclear) with the antibodies indicated in each panel, and reimmunoprecipitated with the p8 antiserum before SDS–PAGE. (B) Phosphoimager quantitation of the band densities in A. The data sets for each pulse–chase were normalized around the 60 min chase point densities.