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  • 1
    Electronic Resource
    Electronic Resource
    Oxidative Coupling of Diphenylmethanimine Catalyzed by Copper-Loaded Copolymers of 4-Vinylpyridine and Divinylbenzene (1978)
    s.l. : American Chemical Society
    Industrial and engineering chemistry 17 (1978), S. 128-133 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/i360066a008
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  • 2
    Electronic Resource
    Electronic Resource
    Aggregation states and catalytic properties of the multienzyme complex catalyzing the initial steps of pyrimidine biosynthesis in rat liver (1975)
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 2622-2630 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00683a010
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  • 3
    Electronic Resource
    Electronic Resource
    Level of translatable messenger RNA coding for argininosuccinate synthetase in the liver of the patients with quantitative-type citrullinemia (1985)
    Springer
    Human genetics 〈Berlin〉 69 (1985), S. 130-134 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The translation activity of mRNA coding for argininosuccinate synthetase in total RNA extracted from the liver of three patients with quantitative-type citrullinemia was determined using a cell-free translation system. In two patients, the hepatic content of the enzyme was about 20% of the control value, whereas translatable mRNA level for the enzyme was similar to or slightly lower than those of control livers. In the third patient, the enzyme content was about 50% of the control value, and mRNA activity for the enzyme was low normal. These results indicate that at least in the first two patients, the decrease in the enzyme protein is due either to increased degradation of the enzyme or to decreased translation in the patient's liver.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293282
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  • 4
    Electronic Resource
    Electronic Resource
    The R40H mutation in a late onset type of human ornithine transcarbamylase deficiency in male patients (1997)
    Springer
    Human genetics 〈Berlin〉 99 (1997), S. 171-176 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Ornithine transcarbamylase (OTC) deficiency is an X-linked trait and is one of the most frequent of the inherited urea cycle enzyme deficiencies. Most male patients with OTC deficiency develop a hyperammonemic crisis and die in the neonatal period or in early infancy. In contrast to those patients, in some male patients the disease first becomes overt in adolescence or during the reproductive age period. In the present report, we describe six such male patients who first developed clinical signs at ages ranging from 6 to 58 years, all of whom came from a limited area of the northern part of Kyushu Island in southern Japan. The mutation analysis disclosed a R40H mutation in exon 2 of the OTC gene in each of these patients. Transmission of this mutant gene through paternal lineage as well as through maternal lineage was documented in one family. The levels of mRNA of the mutant OTC gene expressed in transfected Cos 1 cells and in the liver tissue obtained by biopsy in one patient were both similar to those of the wild-type gene. The activity of the mutant OTC was, however, decreased to a level of 28% of the wild-type OTC, and the levels of the mutant OTC protein expressed in Cos 1 cells were decreased, as assessed by western blot analysis. Apparent K m values of the mutant enzyme for ornithine (1.1 mM) and carbamylophosphate (2.0 mM) were similar to those of the wild-type enzyme. Both enzymes gave similar pH-dependency profiles, giving a maximal activity at pH 7.8–7.9. Activity of wild-type OTC expressed in Cos 1 cells did not change after five cycles of freezing and thawing, whereas that of the mutant OTC decreased to 17% by this treatment. These results suggest that deficiency is due to inactivation of the mutant OTC under certain conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050333
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  • 5
    Electronic Resource
    Electronic Resource
    Ornithine transcarbamylase in liver mitochondria (1982)
    Springer
    Molecular and cellular biochemistry 49 (1982), S. 97-111 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Ornithine transcarbamylase (ornithine carbamoyltransferase, EC 2.1.3.3), the second enzyme of urea synthesis, is localized in the matrix of liver mitochondria of ureotelic animals. The enzyme is encoded by a nuclear gene, synthesized outside the mitochondria, and must then be transported into the organelle. The rat liver enzyme is initially synthesized on membrane-free polysomes in the form of a larger precursor with an amino-terminal extension of 3 400–4 000 daltons. In rat liver slices and isolated rat hepatocytes, the pulse-labeled precursor is first released into the cytosol and is then transported with a half life of 1 2 min into the mitochondria where it is proteolytically processed to the mature form of the enzyme. The precursor synthesized in vitro exists in a highly aggregated form and has a conformation different from that of the mature enzyme. The precursor has an isoelectric point (pI = 7.9) higher than that of the mature enzyme (pI = 7.2). The precursor synthesized in vitro can be taken up and processed to the mature enzyme by isolated rat liver mitochondria. The mitochondrial transport and processing system requires membrane potential and a high integrity of the mitochondria. The transport and processing activities are conserved between mammals and birds or amphibians and is presumably common to more than one precursor. Potassium ion, magnesium ion, and probably a cytosolic protein(s), in addition to the transcarbamylase precursor and the mitochondria, are required for the maximal transport and processing of the precursor. A mitochondrial matrix protease which converts the precursor to a product intermediate in size between the precursor and the mature subunit has been highly purified. The protease has an estimated molecular weight of 108 000 and an optimal pH of 7.5–8.0, and appears to be a metal protease. The protease does not cleave several of the protein and peptide substrates tested. The role of this protease in the precursor processing remains to be elucidated. Rats subjected to different levels of protein intake and to fasting show significant changes in the level of enzyme protein and activity of ornithine transcarbamylase. The dietary-dependent changes in the enzyme level are due mainly to an altered level of functional mRNA for the enzyme. In contrast, during fasting, the increase in the enzyme level is associated with a decreased level of translatable mRNA forthe enzyme. Pathological aspects of ornithine transcarbamylase including the enzyme deficiency and reduced activities of the enzyme in Reye's syndrome are also described. A possibility that impaired transport of the enzyme precursor into the mitochondria leads to a reduced enzyme activity, is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00242488
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  • 6
    Electronic Resource
    Electronic Resource
    Behavioral responses of malePeriplaneta americana L. to female sex pheromone components, periplanone-A and periplanone-B (1990)
    Springer
    Journal of chemical ecology 16 (1990), S. 2605-2614 
    Details
    ISSN: 1573-1561
    Keywords: Periplaneta americana ; sex pheromone ; Orthoptera ; Blattidae ; periplanone-A ; periplanone-B ; American cockroach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Bioassays were performed on malePeriplaneta americana L. using synthetic (−)-periplanone-B (P-B) and Hauptmann's (−)-periplanone-A (P-A), and their mixtures at various ratios to estimate the roles of both periplanones for the sexual communication of the species. Both P-A and P-B elicited qualitatively the same responses, such as antennal movement, rapid locomotion, wing raising, and homosexual behavior of male cockroaches, but the threshold of the pheromone activities for P-B was two orders of magnitude lower than that of P-A. Neither synergistic nor inhibitory but only a simple integrated effect on the responses was observed when mixtures of P-A and P-B were applied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00988072
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  • 7
    Electronic Resource
    Electronic Resource
    Immunohistochemical Localization of Arginase II and Other Enzymes of Arginine Metabolism in Rat Kidney and Liver (1998)
    Springer
    Journal of molecular histology 30 (1998), S. 741-751 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Arginine is a precursor for the synthesis of urea, polyamines, creatine phosphate, nitric oxide and proteins. It is synthesized from ornithine by argininosuccinate synthetase and argininosuccinate lyase and is degraded by arginase, which consists of a liver-type (arginase I) and a non-hepatic type (arginase II). Recently, cDNAs for human and rat arginase II have been isolated. In this study, immunocytochemical analysis showed that human arginase II expressed in COS-7 cells was localized in the mitochondria. Arginase II mRNA was abundant in the rat small intestine and kidney. In the kidney, argininosuccinate synthetase and lyase were immunostained in the cortex, intensely in proximal tubules and much less intensely in distal tubules. In contrast, arginase II was stained intensely in the outer stripes of the outer medulla, presumably in the proximal straight tubules, and in a subpopulation of the proximal tubules in the cortex. Immunostaining of serial sections of the kidney showed that argininosuccinate synthetase and arginase II were collocalized in a subpopulation of proximal tubules in the cortex, whereas only the synthetase, but not arginase II, was present in another subpopulation of proximal tubules. In the liver, all the enzymes of the urea cycle, i.e. carbamylphosphate synthetase I, ornithine transcarbamylase, argininosuccinate synthetase and lyase and arginase I, showed similar zonation patterns with staining more intense in periportal hepatocytes than in pericentral hepatocytes, although zonation of ornithine transcarbamylase was much less prominent. The implications of these results are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1003468726969
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  • 8
    Electronic Resource
    Electronic Resource
    Conformational analysis of serricornin: Application of molecular mechanics calculations to stereochemical assignment of serricornin, sex pheromone of cigarette beetle (Lasioderma serricorne F.) (1990)
    Springer
    Journal of chemical ecology 16 (1990), S. 2877-2888 
    Details
    ISSN: 1573-1561
    Keywords: Conformational analysis ; molecular mechanics ; determination of absolute configuration ; sex pheromone ; Lasioderma serricorne F. ; Coleoptera, Anobiidae ; cigarette beetle ; serricornin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Conformational analysis using molecular mechanics (MM) was performed for a determination of the stereochemistry of serricornin, the sex pheromone of the cigarette beetle (Lasioderma serricorne F.). An exhaustive conformational analysis using MM2 calculations with algorithms for covering torsional energy surfaces of flexible molecules furnishes coordinates and steric energies of all local energy minimum conformers of serricornin, both acyclic and the corresponding cyclic forms. These coordinates gave angles required for the calculation of vicinal H/H coupling constants (3 J HHs) of each energy minima by Altona's modified Karplus equation. The Boltzmann distributions of all local energy minima were calculated from their steric energies to furnish populations of each energy minimum conformer. Populationweighted averaged3 J HHs of four enantiomeric pairs, (S *,S *,S *)-, (S *,S *,R *)-, (S *,R *,S *)-, and (R *,S *,S *)-serricornins were calculated from the data above. The observed3 J HHs of the naturally occurring serricornin, both acyclic and cyclic forms, are fitted best to calcd.3 J HHs of (4S *, 6S *, 7S *)-acyclic and (3S *, 5S *, 6S *)-cyclic serricornin, respectively, among those of four enantiomeric pairs of serricornin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00979480
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  • 9
    Electronic Resource
    Electronic Resource
    Behavioral and electroantennogram responses of periplanone analogs (1991)
    Springer
    Journal of chemical ecology 17 (1991), S. 695-706 
    Details
    ISSN: 1573-1561
    Keywords: American cockroach ; Periplaneta americana ; Orthoptera ; Blattidae ; pheromone ; mimics ; analog ; electroantennogram ; EAG ; bioassays ; periplanone analogs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The biological activities of synthetic periplanone analogs, including four candidates of periplanone-A (P-A), were evaluated by behavioral and electroantennogram (EAG) assays. Among 16 periplanone analogs, six compounds evoked pheromonal activity from the male American cockroaches. The threshold dosages of these biological active analogs were 10–105 times lower than that of the known periplanone mimic, germacrene-D. The conformation required for eliciting the pheromonal activity is discussed in terms of the structure-activity relationship of these analogs. Hauptmann's P-A elicited the strongest pheromonal activity among four candidates of P-A in our bioassay, suggesting that Hauptmann's P-A is a natural P-A produced from female cockroaches.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00994193
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  • 10
    Electronic Resource
    Electronic Resource
    Lasioderma chemistry sex pheromone of cigarette beetle (Lasioderma serricorne F.) (1985)
    Springer
    Journal of chemical ecology 11 (1985), S. 417-434 
    Details
    ISSN: 1573-1561
    Keywords: Sex pheromone ; Lasioderma serricorne F. ; cigarette beetle ; Coleoptera ; Anobiidae ; serricornin ; polyketide biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A chemical study of the sex pheromone of the cigarette beetle was carried out. Seven components were isolated from active fractions of column chromatography of the female extract, and their structures were elucidated by spectroscopic evidence and confirmed by synthesis to be (4S,6S,7S)-4,6-di-methyl-7-hydroxynonan-3-one (serricornin) (I), 2,6-diethyl-3,5-dimethyl-3,4-dihydro-2H-pyran (anhydroserricornin) (II), 4,6-dimethylnonan-3,7-dione (III), 4,6-dimethylnonan-3,7-diol (IV), 4,6-dimethyl-7-hydroxy-4-nonen-3-one (V), (2S,3R)-2,3-dihydro-3,5-dimethyl-2-ethyl-6-(l-methyl-2-oxobutyl)-4H-pyran-4-one (serricorone) (VI) and (2S,3R)-2,3-dihydro-3,5-dimethyl-2-ethyl-6-(1-methyl-2-hydroxybutyl)-4H-pyran-4-one (serricorole) (VII). These structural features suggested that the occurrence of these components might be related to the polyketide biosynthesis. The behavioral bioassay and BAG experiments revealed the biological role of each component in the copulatory behavior of this insect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00989553
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