Elbert E. Harris

Dipeptide mimics. Conformationally restricted inhibitors of angiotensin-converting enzyme

A series of potent inhibitors of angiotensin-converting enzyme (dipeptidyl carboxy-peptidase, E.C. 3.4.15.1) is described which addresses conformational aspects of the enzyme-inhibitor interaction. Conformational probes were derived from simple lactams containing the required recognition and binding elements. The inhibitor potencies vary with lactam ring size in a manner predicted from molecular modeling studies and help map the active site of this important enzyme.

Polynucleotide phosphorylase covalently bound to cellulose and its use in the preparation of homopolynucleotides

Abstract A readily prepared, crude concentrate of polynucleotide phosphorylase (PNPase) has been covalently bound by the method of Porath to cyanogen bromide-activated cellulose; this is the first report of a synthesizing enzyme bound to a solid support. The bound enzyme had good activity and stability; more than forty consecutive polymerization cycles of nucleoside diphosphates have been carried out with a single preparation to give consistently good yields of stable polymers, and these were readily separated from the bound phosphorylase without tedious phenol extractions.