Insulin is produced from an inactive precursor, proinsulin, through initial endoproteolytic
cleavage at sites marked by pairs of basic amino-acid residues1, 2. We report here that …

Exposure of insulin to insulin protease (insulinase, EC 3.4. 22.11), a degradative enzyme
with considerable specificity toward insulin, results in alterations in the properties of the …

Two Ca (2+)-dependent endopeptidase activities are involved in proinsulin to insulin
conversion: type I cleaves COOH-terminal to proinsulin Arg31-Arg32 (B-chain/C-peptide …

Insulin is synthesized in the pancreatic beta cell via a series of precursor proteins which
include preproinsulin and proinsulin. Preproinsulin carries additional information to target …

Proinsulin is converted to insulin in an impure secretion granule fraction prepared from rat
islets of Langerhans that have been labeled before homogenization with [3 H] leucine or [3 …

The endosomal compartment of hepatic parenchymal cells contains an acidic
endopeptidase, endosomal acidic insulinase, which hydrolyzes internalized insulin and …

Insulin consists of two polypeptide chains, A (21 amino acids) and B (30 amino acids), linked
by disulphide bonds. Both chains are derived from one precursor, proinsulin, which includes …

The insulin storage granule of the pancreatic beta cell is assembled within the trans Golgi
network from around 50 or so gene products many of which are synthesized coordinately …

A proteinase with high affinity for insulin has been proposed to play a role in the cellular
processing of this hormone. A complementary DNA (cDNA) coding for this enzyme has been …

Proinsulin is a single polypeptide chain composed of the B and A subunits of insulin joined
by the C-peptide region. Proinsulin is converted to insulin during the maturation of secretory …