Immunohistochemical Localization of Amylase in Peri- and Tele-Insular Acinar Cells of the Human Exocrine Pancreas

An immunohistochemical localization of amylase was demonstrated in human pancreatic acinar cells using a commercial anti-human pancreatic amylase antibody. The immunofluorescence was mainly localized in the cell apices, and some differences in the intensity of the fluorescence was observed among the acinar cells in respect to their location from the islets of Langerhans. The peri-insular acinar cells showed a brighter fluorescence than the cells of tele-insular acini. This inhomogeneity of pancreatic amylase distribution in the human exocrine pancreas adds a further clue to the concept of insulo-acinar interaction.This study was supported by the Japanese Government Scholarship Program for Foreign Students from the Ministry of Education, Science and Culture, Japan

Physicochemical investigation of the reactions of some organo-phosphine derivatives with cyanogen halides

951-953The organo-phosphines CH3P(C6H5)2, (CH3)2P C6H5 and [(C2H5)2N]3 react with CNX(X = I and Br) in methyl cyanide solution to give two adducts, a 1: 1 of ionic nature and 2: 1 non-electrolyte, namely R3PCNI and R3P(CN)2 respectively with CNI, whereas cyanogen bromide gives only one type of adduct of composition R3PCNBr. Conductometric titration studies and molar conductance measurements show that the 1:1 adducts are very strong electrolytes. In contrast, the 2:1 adduct formed in the case of CNI is a non-electrolyte