We will continue our studies on the enzymology of certain peptide hormones: Angiotensin I, atrial natriuretic peptides, hypothalmic gonadotropin releasing hormone (GnRH), and GnRH associated peptide (GAP) which may be prolactin releasing inhibiting hormone.
Our aims are: 1. To determine the catalytic role of the active site glutamic acid of converting enzyme and to determine the nature of the active site. To explain substrate inhibition and noncompetitive inhibition. To study the nature of the shift in the cleavage site. 2. To sequence converting enzyme from its cDNA. 3. To purify and study atrial PDH (recently discovered in this laboratory) with respect to its role in processing the C termini of atrial natriuretic peptides. To see if it contains an active site glutamic acid. 4. To chemically sequence a very small active site peptide of atrial PDH and to sequence about 200 amino acids of the active site from cDNA. 5. To purify and study an enzyme (recently discovered in this laboratory) that processes the N terminus of atrial natriuretic peptides. 6. To purify and study GAP releasing enzyme (recently discovered in this laboratory) in relationship to its physiological role. 7. To look for enzyme(s) that process the C terminus of GnRH.
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