Kallikrein content of rat pancreatic acinar cells or islets by direct radioimmunoassay.
Recent reports have suggested that kallikreins may enzymatically convert proinsulin to insulin. The quantity of rat pancreatic kallikrein in isolated Islets of Langerhans, acinar cells and in whole pancreatic extracts was measured by direct radioimmunoassay and bioassay. Immunoreactive kallikrein content in acinar cells was 813 +/- 111 ng/mg protein (mean +/- S.E.M.). In whole pancreatic homogenates, it was 1303 +/- 213 ng/mg protein. Appreciable quantities of the enzyme were not detected in islets. Kallikrein activity as measured with a rat uterine bioassay had similar distribution. Because of the localization of kallikrein, it is unlikely that the enzyme is involved in the in vivo conversion of proinsulin to insulin.
D000818:Animals; D005260:Female; D066298:In Vitro Techniques; D007515:Islets of Langerhans / Q000201:enzymology*; D007610:Kallikreins / Q000032:analysis* / Q000652:urine; D008297:Male; D010179:Pancreas / Q000201:enzymology*; D011506:Proteins / Q000032:analysis; D011863:Radioimmunoassay / Q000379:methods; D051381:Rats; D014590:Uterine Contraction / Q000187:drug effects
D011506:Proteins; D007610:Kallikreins