The sequence of two peptides isolated from the Ca2+-transporting ATPase of rabbit sarcoplasmic reticulum after cleavage at tryptophan.
Cleavage of reduced, carboxymethylated, delipidated CA2+-transporting ATPase protein from rabbit sarcoplasmic reticulum with dimethyl sulphoxide/HBr yielded two long peptides (38 and 73 residues), distinct from the known major sequences of the ATPase. The longer peptide contained at least two cysteine residues, which were disulphide-linked in the native protein. It was therefore derived from the B-fragment of the ATPase in which the disulphides had previously been located. It probably formed a loop on the luminal side of the membrane, spanning two membrane-buried tryptophan residues. The N-terminal sequence of this peptide, (Trp)-Phe-Met-Tyr-Ala, forms the basis for an oligodeoxynucleotide probe, the use of which to identify cDNA corresponding to the ATPase is described elsewhere [MacLennan, Brandl, Korczak & Green (1985) Nature (London) 316, 696-700].
Green
N M
NM
Toms
E J
EJ
D000595:Amino Acid Sequence; D000818:Animals; D000252:Calcium-Transporting ATPases; D004121:Dimethyl Sulfoxide; D010446:Peptide Fragments / Q000032:analysis* / Q000302:isolation & purification; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D014364:Tryptophan
D010446:Peptide Fragments; D014364:Tryptophan; D000252:Calcium-Transporting ATPases; D004121:Dimethyl Sulfoxide