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. 1997 Jun 30;137(7):1483–1493. doi: 10.1083/jcb.137.7.1483

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BiP solubilized from yeast microsomes binds to 63Jp in an ATP- dependent manner. Soluble proteins from microsomes solubilized with Triton X-100 were mixed with a glutathione agarose 63Jp affinity matrix either with 1 mM ATP (+ ATP) or no ATP (− ATP) added. Binding reactions were at pH 6.8. The top panel is a 12.5% SDS–polyacrylamide gel stained with Coomassie brilliant blue R-250. Molecular mass markers (in kD) are on the left. P, insoluble microsomal proteins (pellet); FT, proteins not bound to affinity matrix (flow through); W, wash fractions; B, proteins still bound to beads after washing. The bottom panel is the region between 97 and 66 kD of an immunoblot probed with anti-BiP antibody.