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note
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Membrane proteins extracted from salt-washed rat liver Golgi membranes (6) were incubated with CNBr-Sepharose conjugated with mAb HFD9. p28 eluted from the beads was subjected to trypsin or endoproteinase GluC digestion. The resulting peptides were sequenced with a model 6600 ProSequencer (Milligen, Burlington, MA). One cDNA fragment of about 400 bp was obtained by PCR with a sense oligonucleotide [GA(T/C)AT(T/C/A)(T/C)TI-CA(A/G)GA(T/C)TA(T/C)ACICA] to peptide P4 (DILDYQTHE) and an antisense oligonucleotide [TG(A/G/T)ATIA(A/G)I(C/G)(A/T)(A/G)TTIACAGCIGG (A/G)AA] to peptide P9 (FPAVNSLIQR). This cDNA fragment was used to isolate a full-length rat cDNA clone (SKT7p28). Database searches were done with the BLAST program.
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Transport assay was done exactly as described [C. J. M. Beckers, D. S. Keller, W. E. Balch, Cell 50, 523 (1987); H. W. Davidson and W. E. Balch, J. Biol. Chem. 268, 4216 (1993)].
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Balch, W.E.3
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Transport assay was done exactly as described [C. J. M. Beckers, D. S. Keller, W. E. Balch, Cell 50, 523 (1987); H. W. Davidson and W. E. Balch, J. Biol. Chem. 268, 4216 (1993)].
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15844422914
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note
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The coding regions of p28cyto and cellubrevin minus the COOH-terminal transmembrane regions were amplified and cloned into pET23(d) (Novagen). This vector yields recombinant proteins with a COOH-terminal hexahistidine tag. Proteins were purified as recommended by the manufacturer.
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15844402609
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note
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6-α-SNAP in a final volume of 500 μl. After a 30-min incubation at 4°C, the samples were loaded onto a 15 to 40% (w/v) glycerol gradient in the assembly (Flj. 4A) (a and b) or the disassembly buffer (c). Centrifugation was carried out for 18 hours in a SW41 rotor (Beckman). Fractions of about 0.8 ml were collected manually from the bottom at a flow rate of ∼1 ml/min. Samples were resolved by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), and the distribution of p28 was determined by immunoblotting.
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15844374018
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note
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2, and 25 μm guanosine triphosphate (GTP)]. The beads and supernatants were then processed for immunoblotting with antibodies to p28, α-SNAP, and NSF.
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note
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We thank J. E. Rothman and W. E. Balch for re-agents, C. Pallen, W. Chia, and members of W. Hong's laboratory for critical reading of the manuscript, and Y. H. Tan for his continuous support.
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