High-resolution 1H NMR study of membrane phospholipids in rat pancreas stimulated by caerulein.

In this study, the peak observed at 3.2 +/- 0.2 ppm in the 1H nuclear magnetic resonance (NMR) spectra recorded at 60 MHz of rat pancreas stimulated by caerulein was characterized at higher resolution (100 and 300 MHz).

Creatine phosphate as energy source in the cerulein-stimulated rat pancreas study by 31P nuclear magnetic resonance.

Stimulation of the rat exocrine pancreas by cerulein induces a variety of cellular processes, some of which require the expenditure of energy. In this study, changes in the amounts of various energy metabolites, including creatine phosphate (PCr), ATP, and ADP were determined by high-resolution 31P NMR spectroscopy. The spectrum of a perchloric acid extract of pancreas from the 48 h fasted rat was taken as a reference for comparison of 31P NMR spectra recorded after stimulation by cerulein.

Culture of islets of Langerhans from an infant with intractable neonatal hypoglycemia: cytochemical and radioimmunological studies.

Extralobular islet of Langerhans cells were isolated from the pancreas of an infant with intractable neonatal hypoglycemia (nesidioblastosis) by digestion with a mixture of trypsin and collagenase, and subsequent purification on a gradient of fetal calf serum. These islet cells cultured in Eagle's medium containing 20% fetal calf serum formed confluent endocrine cell monolayers within 15 days. These endocrine cells were studied immunocytochemically, and their secretion products were assayed by radioimmunological methods.

The amiloride sensitive Na+/H+ antiport in guinea pig pancreatic acini. Characterization and stimulation by caerulein.

Amiloride and analogs decrease the initial rate of 22Na+ uptake by dispersed acini from guinea pig pancreas in a dose-dependent manner. The initial rate of amiloride-sensitive 22Na+ uptake depends on external Na+ and H+ concentrations and on internal pH. These results provide evidence for the existence of a Na+/H+ antiport in pancreatic acinar cells.

Covalent attachment of insulin to the outer surface of liposomes.

We describe a method for covalent binding of insulin to the outer surface of multilamellar liposomes loaded with spin label. Encapsulation of the label Tempocholine-nitroxide within the aqueous phases of liposomes is controlled by Electron Spin Resonance. The binding of insulin is performed using the Carlsson's heterobifunctional reagent: N-succinimidyl 3-(2-pyridyldithio) propionate.