Fig. 1.
Fig. 1. Autoradiograph of various proteolytic fragments of CDB3 phosphorylated by casein kinase I and [δ-32P]ATP. CDB3 was phosphorylated by casein kinase I using radiolabeled ATP, as described in the Materials and Methods. Phosphorylated CDB3 was then either left unmodified or digested at specific sites and separated by Tricine SDS-PAGE. Lane A, intact CDB3; lane B, proteolytic fragments generated by NTCB cleavage; lane C, fragments produced by NH2OH hydrolysis; and lane D, fragments released upon digestion in formic acid. Lane E shows the position of molecular weight markers.

Autoradiograph of various proteolytic fragments of CDB3 phosphorylated by casein kinase I and [δ-32P]ATP. CDB3 was phosphorylated by casein kinase I using radiolabeled ATP, as described in the Materials and Methods. Phosphorylated CDB3 was then either left unmodified or digested at specific sites and separated by Tricine SDS-PAGE. Lane A, intact CDB3; lane B, proteolytic fragments generated by NTCB cleavage; lane C, fragments produced by NH2OH hydrolysis; and lane D, fragments released upon digestion in formic acid. Lane E shows the position of molecular weight markers.

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