Abstract
The amino-terminal sequence of a hypocalcemic protein purified from bovine parotid gland was determined as Lys-Leu- by the dansyl-Edman method in the presence of sodium dodecyl sulfate (SDS). The amount of amino-terminal lysine was quantified as 0.85 mole per mole of protein. A carboxyl-terminal sequence was analyzed by use of carboxypeptidase A and it was deduced to be-Thr-Val-Leu. Furthermore, the carboxylterminus was confirmed to be leucine alone by the hydrazinolysis method. On SDS gel electrophoresis, this protein failed to show the evidence of dissociation or association. From these results, the hypocalcemic protein was concluded to consist of a single polypeptide chain.
