Biomedical subjects
Publications and source records attributed to M Doi.
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We experienced an autopsy case of alpha-fetoprotein(AFP)-producing advanced gastric carcinoma with liver metastasis. Microscopically, the tumor was compose by medullary nests of poorly differentiated adenocarcinoma cells. The cells had an exclusively hepatoid pattern characterized by discrete masses, nests, and broad bands, consisting of large eosinophilic epithelial cells and separated by fibrous stroma. Immunohistochemical studies of hepatoid cells yielded a positive reaction for AFP, but negative for CEA. Electron microscopically, tumor cells possess a ductal lumina with abundant microvilli having a central core filaments, and secretory granules in cytoplasma. These findings suggest that the tumor cells differentiated into intestinal direction, irrespective of the appearance of their hepatoid features characterized by light microscopy.
The conformation of six amidine compounds, which possess a common 3-[(4-thiazolyl)methylthio]propionylamidine framework but exhibit different activities as histamine H2-receptor antagonists, have been subjected to both single crystal X-ray structural and 1H-NMR analyses. The X-ray studies suggest a correlation between antagonist activity and the relative spatial orientation of the thiazolyl and amidine nitrogen atoms. This correlation is supported by a comparison of the conformations observed for the amidines with those of other H2-receptor antagonists and reveal that a folded conformation, specifically the NH...N intramolecular hydrogen-bonded configuration, is important for antagonist activity. The 1H-NMR measurements on the active amidine compounds show that the intramolecular NH...N bond is likely to be present in solution.
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The respiratory effects of sevoflurane were studied in seven patients and compared with values obtained in another seven patients anesthetized with halothane. Resting ventilation, resting PaCO2, and ventilatory response to CO2 were measured awake and at 1.1 and 1.4 MAC levels of both anesthetic agents. We found that with sevoflurane, tidal volume and the slopes of the CO2 response curves decreased and PaCO2 increased with increasing depth of anesthesia, as with other inhaled anesthetics. A compensatory increase in respiratory frequency was not enough to prevent a decrease in minute volume with increasing depth of anesthesia. At 1.1 MAC, sevoflurane produced almost the same degree of respiratory depression as halothane. At 1.4 MAC, sevoflurane produced more profound respiratory depression than halothane.
Benzoyl-L-arginine p-nitroanilide hydrolase in the etiolated leaves of Zea mays L. has been purified 1,266-fold by a combination of gel filtration, ion exchange, and hydrophobic chromatography with a recovery of 13%. The specific activity of the purified enzyme is 5.7 units/mg protein. The enzyme is an acidic protein with a pI value of 4.6 and optimum pH of 8.2. The molecular weight of the enzyme was estimated to be 59,000. Substrate inhibition was observed at a concentration higher than 30 microM BAPA and the apparent Km for BAPA was 29 microM at pH 8.0. The enzyme activity was inhibited by sulfhydryl reagents, leupeptin, antipain, and N-tosyl-L-lysine chloromethyl ketone. The inhibitor study suggests that the enzyme belongs to the class of the sulfhydryl proteases.
The crystal structure of title complex has been analyzed by X-ray diffraction method as a model for elucidating the possible interaction between the phenylalanyl residue of proteins and the N7-protonated or methylated guanine base of nucleic acids. The guanine base is associated with the benzene ring of phenylalanine by stacking interaction, and further connected with the carboxyl group by the formation of a pair of hydrogen bonds. These two interaction modes are suggested to be responsible for the specific recognition of base sequence by protein.
Strong pi-pi stacking interaction between the indole ring and 7-methylguanine base was shown by X-ray crystal analysis of the 7-methylguanosine 5'-monophosphate-tryptamine complex. This interaction appears to be strengthened by the attachment of ribose and phosphate groups to the base.
7 alpha-Formylamino-1-oxacephalosporins 7 alpha-formylamino-7 beta-[2- (methylaminocarbonyl)amino-2-(2-thienyl)acetamido]-3-[(1-methyl-1H -tetra zol-5-yl)thiomethyl]-1-oxa-3-cephem-4-carboxylic acid (F1) and 7 alpha-formylamino-7 beta-(2-[(4-ethyl-2,3-dioxopiperazine-1- yl)carbonylamino]-2-phenylacetamido)-3-[(1-methyl-1H-tetr azol-5-yl) thiomethyl]-1-oxa-3-cephem-4-carboxylic acid (F2) were stable against penicillinases and, moreover, inactivated cephalosporinases of Pseudomonas aeruginosa, Citrobacter freundii, and Enterobacter cloacae. Extensive studies of the inactivation of cephalosporinase of P. aeruginosa showed that it resulted from the formation of a transiently stable enzyme-compound complex. The 7 alpha-formylamino substituent was involved in the enzyme inactivation, because 7 alpha-methoxy congeners did not inactivate the enzyme. The number of compound molecules required for inhibition of an enzyme molecule was found to be 36 for F1 and 5.5 for F2, which suggests that the pathway to the complex formation branched off the hydrolysis pathway. Half-lives of the complexes were 400 min for F1 and 260 min for F2. 7 alpha-Formylamino compounds F1 and F2 had antibacterial activities similar to those of 7 alpha-methoxy congeners against beta-lactamase-producing gram-negative bacteria, whereas they were less active against non-beta-lactamase-producing strains of Escherichia coli and Staphylococcus aureus. The conclusion was that the 7 alpha-formylamino substituent conferred the ability to inactivate cephalosporinase on the 1-oxacephalosporins tested, without much impairment of their antibacterial activity.
A novel penicillin-binding protein, PBP-2' (Mr about 75,000), is known to be induced in excessively large amount by most beta-lactam compounds in cells of a clinically isolated strain of Staphylococcus aureus, TK784, that is highly resistant to beta-lactams and also most other antibiotics. This protein has very low affinities to most beta-lactam compounds and has been supposed to be the cause of the resistance of the cells to beta-lactams. A 14-kilobase DNA fragment was isolated from the cells that carried the gene encoding this penicillin-binding protein and also a genetically linked marker that is responsible for the resistance to tobramycin. This DNA was cloned on plasmid pACYC184 and was shown to cause both production of PBP-2' and resistance to tobramycin in Escherichia coli cells. However, the formation of PBP-2' in E. coli was only moderate and was independent of normal inducer beta-lactams. The PBP-2' formed in the E. coli cells showed slow kinetics of binding to beta-lactams similar to that of PBP-2' formed in the original S. aureus cells and gave a similar pattern of peptides to the latter when digested with the proteolytic V8 enzyme of S. aureus.
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