PURIFICATION AND THE PARTIAL AMINO-ACID-SEQUENCE OF A NOVEL ACTIVATOROF RYANODINE RECEPTOR (BMK AS-1) FROM MAMMALIAN SKELETAL-MUSCLE

BmK AS-1, a new activator of ryanodine receptor on skeletal muscle, ha s been purified from the venom of scorpion Buthus martensi Karsch. The purified BmK AS-1 gave a single band with molecular weight of approxi mately 8,000 Da on SDS-PAGE. The molecular weight of the peptide was f urther determined to be 7,708 Da electrospray mass spectroscopy (ESMS) . The partial amino acid sequence of N-terminal 16 amino acid residues (except two residues at positions 13 and 15) of BmK AS-1 has been det ermined. The N-terminal 1-16 sequences of BmK AS-1 differs at two posi tions, 7 and 14, from those of BmK AS which was reported previously.