| abstract |
Peptidyl-glycine ~-amidating monooxygenase is an enzyme extractable from medullary thyroid carcinoma cell lines and tissue samples, having a molecular mass of about 60,000 to 65,000 daltons. It has been purified so as to exhibit a single, homogeneous, well-defined band using electrophoretic procedures performed on SDS-polyacrylamide gels, and has a specific enzymatic activity of at least 50mU per mg protein. The free or immobilized enzyme, in the presence of Cu+2 ions, ascorbate, and oxygen, can be used to prepare an ~-amidated protein from a polypeptide substrate possessing a carboxyl-terminal glycine residue. The purified enzyme can be used as an antigen in order to produce enzyme-specific monoclonal antibodies, and can provide the information necessary to design and construct prokaryotes or other appropriate unicellular organisms or host cells isolated from multicellular organisms which possess peptidyl-glycine ~-amidating capability. |