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Fig. 2. Immunoblots of (white-eyed) wild type (WT), null mutant Csp^U1w (U1), cDna1-rescued null mutant (cDNA1), and transgenic mutants (serine string protein (SSP), cysteine-less protein (CLP), linker deletion (C8), C-terminal deletion (C27), cysteine stringless protein (CSLP), and short cysteine string protein (SCSP), all except for CSLP in B in Csp^U1w genetic background. Vertical dotted lines separate lanes of different mutants and vertical solid lines separate different blots. The SAP47-marked signals represent loading controls. Blots were developed with mAbs DCSP1 (DCSP2 when C27 was loaded) and mAb nc46 for detection of SAP47. (A) Heads homogenized in SDS buffer, 1–2 heads per lane. The leftmost WT lane was from a large gel for improved separation and has been graphically compressed for comparison with the small gel lanes. (B) Heads were homogenized in buffer A, a post-nuclear supernatant (S1) was fractionated by ultracentrifugation to separate soluble proteins (S2) from membrane or cytoskeleton associated proteins (P2). Wild-type CSPs (WT, cDNA1), L8, C27 and SCSP are detected exclusively in the membrane fraction, CSLP (analyzed here in WT background as control) is present in both fractions, whereas CLP and SSP are seen only in the soluble fraction. A single WT head homogenized in SDS buffer is shown for comparison (H). (C) Pellets P1 were deacylated with hydroxylamine and ultracentrifuged to obtain supernatant S3 and pellet P3. A smaller protein after deacylation (P3) indicates the loss of palmityl residues in wild-type CSPs (WT, cDNA1), L8, C27 and SCSP. 32, position of the 32 kDa marker protein.

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