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A case of adenocarcinoma arising in Meckel's diverticulum in a 55 year old man is reported, and a brief review of the literature is presented. The patient developed low abdominal pain and showed elevation of serum carcinoembryonic antigen (CEA) level. The tumour was located in the apical portion of the diverticulum and extended into the mesenterium. Histologically, the tumour was a well‐differentiated adenocarcinoma arising in the Meckel's diverticulum. Immunohistochemical study showed that malignant cells were positive for CEA. The noteworthy feature of this case is the pre‐operative elevation of serum CEA level and the immunohistochemical demonstration of CEA in the cancer cells.

Pmr Structure Analysis of Poly(propylene oxide) 459 should be the most probable of the pentads deriving from BAA triads. Similar observations can be made for every peak in the spectrum; again, the observed frequences correspond to the calculated pentad sequences with higher ethylene content. Owing to the low number of transients presently used we think that an analysis at even lower vinyl acetate content is possible; experiments on polymers containing a very small amount of each monomer are in progress.Another interesting result is given by the spectrum of the copolymer with 0.18-mol fraction vinyl acetate obtained using a solid sample (Figure 4). Fine structure is present similar to that obtained with the same sample in benzene solution. The carbonyl signal (not shown in Fig-ure 4) appears to be shifted in respect to the corresponding signal in solution, respectively at 11.2 and 24.8 ppm, showing the shielding effect of the aromatic solvent. Other chemical shifts appear unaffected. Further experiments on solid samples are in progress. Although this result must be considered in greater detail, the possibility of obtaining data for such a polymer in the solid state is evident. Aknowledgment. This work was sponsored by the Consiglio Nazionale delle Ricerche. The authors thank Dr. F. Wehrly of Varían for running the spectra.

Physiological activity of G protein gated inward rectifier K+ (GIRK, Kir3) channel, dynamically regulated by three key ligands, phosphoinositol-4,5-bisphosphate (PIP2), Gβγ, and Na+, underlies cellular electrical response to multiple hormones and neurotransmitters in myocytes and neurons. In a reducing environment, matching that inside cells, purified GIRK2 (Kir3.2) channels demonstrate low basal activity, and expected sensitivity to the above ligands. However, under oxidizing conditions, anomalous behavior emerges, including rapid loss of PIP2 and Na+-dependent activation and a high basal activity in the absence of any agonists, that is now paradoxically inhibited by PIP2. Mutagenesis identifies two cysteine residues (C65 and C190) as being responsible for the loss of PIP2 and Na+-dependent activity and the elevated basal activity, respectively. The results explain anomalous findings from earlier studies and illustrate the potential pathophysiologic consequences of oxidation on GIRK channel function, as well as providing insight to reversed ligand-dependence of Kir and KirBac channels.