Taste receptor stimulation and feeding behaviour in the puffer, Fugu pardalis. II. Effects produced by mixtures of constituents of clam extracts

The effects of extracts of short-necked clam, Tapes japonica,as feeding stimulants on the puffer, Fugu pardalis, were studiedby applying the constituents of the extracts in starch pellets.As observed elsewhere (Hidaka et al., 1978), the starch pelletcontaining all the constituents found in the clam extracts (Konosuet al., 1965), except homarine and choline, at the same concentrationratios as in the clam tissue was taken up by the fish. Omissiontests on the chemical constituents suggested that the palatabilityof the clam pellet might be largely produced by some amino acidsand betaine: Pellets containing alanine, glycine, proline, serineplus betaine were nearly as effective as those containing allthe extractive compounds except homarine and choline. Mixturesfree of either the above amino acids or betaine tested wereall less effective. The nucleotides and related substances andorganic acids detected in the clam extracts had no appreciableeffect except that a mixture of all of them was weakly acceptedby adding betaine to it. The other amino acids found in theextracts appear to be ineffective.     

Taste receptor stimulation and feeding behaviour in the puffer, Fugu pardalis I. Effect of single chemicals

In electrophysiological experimentation, various chemicals areeffective in stimulating the lip chemoreceptors of the puffer,Fugu pardalis (Hidaka et al., 1975; Kiyohara et al., 1975a).Their effects as feeding stimulants on this fish were studiedby offering the lip stimulants in starch pellets. The starchpellet by itself was not taken by the fish but it was acceptedwhen stimulants such as clam extracts were addded to it. Sucrose,ineffective as a lip chemoreceptor stimulant, had no effecton feeding behaviour. NaCl, to which the lip chemoreceptorsshow a low sensitivity, did not affect the feeding responsewhen added at 2 M to clam extracts. HCl and quinine inhibitedthe response of the fish to the clam extracts. Alanine and otheramino acids, which were effective on the lip chemoreceptors,were accepted. AMP, IMP, UMP and ADP were not accepted in spiteof their marked stimulatory effectiveness on the lip chemoreceptors.Sodium salts of fumaric, malic and succinic acids were not accepted.     

Comparative Studies of NAD-Malic Enzyme from Leaves of Various C4 Plants

Using butyl-TSK-gel chromatography, we purified NAD-malic enzyme(ME) (EC 1.1.1.39 [EC] ), which is involved in C₄ photosynthesis,to electrophoretic homogeneity, from leaves of Amaran-thus tricolor.Molecular weights of the native and SDS-denatured enzyme fromA. tricolor were 490 kDa and 61 kDa, respectively. During assayof the enzyme there was a slow reaction transient in the formof a lag before a steady-state rate was reached. The durationof this lag was inversely proportional to the concentrationof each substrate and the activator, fructose- 1,6-bis-phosphate(FBP). The optimal pH of the reaction fell with decreasing concentrationsof either malate or FBP. High pH prolonged the lag in reaction. Double reciprocal plots of the enzymatic activity as a functionof the concentration of malate yielded straight lines and didnot show any cooperativity for binding of malate. The enzymefrom A. tricolor was not inhibited by either HCO^–₃ orCO₂. At different concentrations of malate, the nature of theactivating effect of FBP was compared among the purified enzymesfrom A. tricolor and the C₄ monocots Eleusine coracana and Panicumdichotomiflorum. At low levels of malate, FBP markedly stimulatedthe enzyme from each species. In contrast, at saturating levelsof malate, the response of enzymes to increasing concentrationsof FBP was different and depended on the source of enzyme. The immunochemical properties of the enzymes from the threespecies were compared using an enzyme-linked immunoadsorbentassay with antisera raised against the purified enzymes fromthe three species. Different cross-reactivities were observedamong the enzymes from different sources. The N-terminal aminoacid sequences of NAD-MEs from the three species were determinedand some differences were found among the three enzymes. ²Permanent address; Tohoku National Agricultural ExperimentStation, Morioka, 020-01 Japan. ³Permanent address; National Grassland Research Institute, Nishinasuno,Tochigi, 329-27 Japan. (Received December 12, 1988; Accepted February 17, 1989)     

Leaf anatomy, post-illumination CO2 burst and NAD-malic enzyme activity of Panicum dichotomiflorum

Light microscopic observation of leaf blades of Panicum dichotomiflorumshowed that a mestome sheath was present and chloroplasts inbundle sheath cells were in the centrifugal position. However,a sharp pattern of post-illumination CO₂ burst was observedin less than 30 sec after the extinction of light. Among threeC₄-acid decarboxylating enzymes, only the activity of NAD-malicenzyme was high. These results indicate that P. dichotomiflorumis a NAD-malic enzyme type species having centrifugal chloroplastsin bundle sheath cells and the sharp pattern of post-illuminationCO₂ burst is closely correlated with the C₄-acid decarboxylationsystem through NAD-malic enzyme ¹This research was supported by a grant from the Ministry ofAgriculture, Forestry and Fishery (GEP55-II-1-7). (Received August 18, 1980; )     

Bacterial translocation from the gastrointestinal tract in various mouse models for human diabetes.

Bacterial translocation from the gastrointestinal (GI) tract to other internal organs was examined in multiple low-dose streptozotocin-injected (M-STZ), single large-dose streptozotocin-injected (S-STZ), alloxan-injected (Alloxan), and non-obese diabetic (NOD) mice. The incidence of bacterial translocation from the GI tract to the tested organs among diabetic mice was in the order of M-STZ mice greater than S-STZ mice greater than NOD, Alloxan, and control mice. The injections of insulin to M-STZ mice did not decrease the incidence of translocation. These results suggest that bacterial translocation from the GI tract in diabetic mice is not induced by diabetes.