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. 1999 Sep 20;146(6):1277–1288. doi: 10.1083/jcb.146.6.1277

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© 1999 The Rockefeller University Press

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graphic file with name JCB9904016.f3a.jpg — Biochemical analysis of KLC1 mutant mice. A, KIF5A or KIF5B antibodies were used in immunoprecipitation experiments and then probed with KIF5A, KIF5B, or 63-90 antibodies to assess the association of KHC and KLC forms in wild-type, heterozygous, and homozygous mutant genotypes. B, Sucrose gradient analysis of high-speed supernatant of brain extracts from wild-type (open circles) and mutant KLC1 (closed circles) was done using 5–20% linear sucrose gradients. 16 fractions were collected (fraction 1 is top of gradient), and equal volumes were loaded for Western analysis. The relative intensity of the bands in each fraction was calculated as described in Fig. 2 D and plotted. Control protein markers were run in parallel gradients; the enzyme activity of alcohol dehydrogenase (7 S) was at fraction 6, catalase (11.3 S) was at fraction 9-10, and β-galactosidase (16 S) was at fraction 13-14 (data not shown).

graphic file with name JCB9904016.f3b.jpg — Biochemical analysis of KLC1 mutant mice. A, KIF5A or KIF5B antibodies were used in immunoprecipitation experiments and then probed with KIF5A, KIF5B, or 63-90 antibodies to assess the association of KHC and KLC forms in wild-type, heterozygous, and homozygous mutant genotypes. B, Sucrose gradient analysis of high-speed supernatant of brain extracts from wild-type (open circles) and mutant KLC1 (closed circles) was done using 5–20% linear sucrose gradients. 16 fractions were collected (fraction 1 is top of gradient), and equal volumes were loaded for Western analysis. The relative intensity of the bands in each fraction was calculated as described in Fig. 2 D and plotted. Control protein markers were run in parallel gradients; the enzyme activity of alcohol dehydrogenase (7 S) was at fraction 6, catalase (11.3 S) was at fraction 9-10, and β-galactosidase (16 S) was at fraction 13-14 (data not shown).