Abstract: A stable pharmaceutical formulation for intravenous or intramuscular administration of Octreotide, which is characterized in that the vehicle for injection of the peptide or pharmaceutically acceptable salts thereof contains glycine in concentrations ranging from 10 to 60 mM and aqueous solution of hydrochloric acid in sufficient quantity to adjust the pH of the formulation to values between 3.0 and 4.2.

Abstract: A stable pharmaceutical formulation for intravenous or intramuscular administration of Octreotide, which is characterised in that the vehicle for injection of the peptide or pharmaceutically acceptable salts thereof contains glycine in concentrations ranging from 10 to 60 mM and aqueous solution of hydrochloric acid in sufficient quantity to adjust the pH of the formulation to values between 3.0 and 4.2.

Abstract: A procedure for obtaining the somatostatin analog, octreotide by means of solid phase synthesis on polymer supports and by intervention of protector groups of the Fmoc/tBu type. It includes construction of the seven amino acid, Boc-D-Phe-Cys(Trt)-Phe-D-Trp-Lys(Boc)Thr(tBu)-Cys(Trt)-Cl-trityl-R linear peptide, in which R is a polymer; treatment of the resulting peptidyl-resin with acid, for detachment of the peptide from the resin; cycling the linear structure obtained by reaction with iodine before or after incorporation of the threoninol residue into the terminal carboxy end; incorporating the threoninol residue in solution upon the seven amino acid protected peptide with or without the disulfide bridge formed; and removing the protections at the N-terminus and at the side chains with a treatment with 70-95% TFA in presence of scavengers to obtain octreotide.

Abstract: A procedure for obtaining carbocalcitonin comprising the condensation of fragment 1, a docosapeptide corresponding to the carboxamide end of the carbocalcitonin sequence, conveniently protected and anchored on resin, with fragment 2 or 3, a nonapeptide corresponding to the amino end of the salmon calcitonin sequence, with a ready-formed cycle between the Asu and Ser residua, and the treatment of the complete peptide skeleton (fragment 6 or 7) with an acid to free the totally deprotected peptide from the resin.