SUMMARY:After effectively eliminating the nonspecific crossimmunoreactivity with the affinity columns of anti-IgG agarose and IgG agarose, the potent immunoreactivities of pll and calcyclin in wheat germ, lobster tail muscle, and three strains of baker's yeast were analyzed by Western blotting using mouse anti-pll and rabbit anti-calcyclin.The occurrence of multiple bands may be due to either autolyses and/or the interactions between the pll (or calcyclin) and other endogenous biological molecules.The results suggest not only a ubiquitous distribution and a universal Ca 2+-mediating regulatory role of pll and calcyclin in eukaryotes, but also an evolutionary conservation of these (S-100)-related proteins.

The interaction between polyadenylic acid (5′) (poly[A]) and histone (or protamine) was analyzed by electrophoretic retardation of poly[A]‐histone (or protamine) complex in agarose gel. The potency of interaction was protamine > histone H1, arginine‐rich histone > other histones. The catalytic subunit of cyclic AMP‐dependent protein kinase effectively decreased the electrophoretic retardation of poly[A]‐histone H1. The interaction between poly[A] and histone H1 was also detected by the drastically enhanced absorbance around 340 nm. The findings may implicate a regulatory role of histone H1 on mRNAs through its binding on poly[A] tails.