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. 1996 Dec 24;93(26):15203–15208. doi: 10.1073/pnas.93.26.15203

Figure 3.

Figure 3

GAIP behaves as an integral membrane protein. Membrane fractions (100,000 × g pellet) from AtT-20 cells stably expressing GAIP (clone 14) were treated with Na2CO3. Proteins were separated by SDS/12% PAGE and immunoblotted. (A) GAIP remains associated with the membrane fraction (P) after Na2CO3 treatment and is not detected in the soluble fraction (S). (B) Cab45, a soluble luminal Golgi protein, is released from the membrane fraction (P) and appears in the supernatant (S) after Na2CO3 treatment.