[Gastrin, cholinergic and alimentary stimulation of gastric acid secretion in awake rabbits with a Heidenham pouch]. / Etude des stimulations gastrinique, cholinergique et alimentaire de la sécrétion gastrique acide d'une poche de Heidenhain chez le lapin éveillé.

Gastric acid secretion was studied in awake rabbits equipped with a Heidenhain pouch. The realisation of a pouch in the rabbit is reported for the first time. Post surgical complications were observed such as shocks, anaesthesia toxic effects, electrolytic impairments, skin burns and gastric ulcers. The continuous gastric secretion and the thinness of the muscularis are mainly responsible for the technical problems not observed in other species. Gastric acid secretion was high during basal periods in rabbits after 24 h of fasting with a collar to prevent any caecotrophia, which gives an empty stomach. It is equivalent to 20% of the acid output produced by pentagastrin (32 micrograms.kg-1.h-1). The highest acid output was obtained during carbaminoylcholine intravenous infusion (20 micrograms.kg-1.h-1) i.e. about twice that induced by pentagastrin. Regular dry diet did not produce any stimulation nor 2 DDG used as a control of complete vagal denervation of the pouch. Unlike in other species, gastric acid secretion of awake rabbit displays a preferential sensitivity to cholinergic stimulants and an insensitivity to regular diet which releases endogenous hormones humorally transmitted to the pouch. The use of rabbit isolated parietal cells or gastric glands to demonstrate the mechanisms of gastric acid secretion, makes it necessary to perform a complete physiological study of gastric secretion in the rabbit with the technique of the isolated pouch we describe here.

Isolation and characterisation of porcine sorbin.

Sorbin has been isolated from extracts of porcine upper intestine, and the biological activity in absorbing water and electrolytes utilized to monitor the purification procedure. Pure sorbin was obtained in a yield of about 1 mg/Mg boiled intestine. The protein chain has 153 amino acid residues and the primary structure was determined by analyses of CNBr-cleaved fragments and four enzymatic digests. The protein has a free N-terminal Met and an amidated C-terminal Ala. No structural similarity was observed with other known proteins in data bases, but several segments have special properties and the C-terminal half is rich in Pro and Arg.