Scanning and transmission electron microscopy of oral sucker papillae of Philophthalmus megalurus

Edwards H. H., Nollen P. M. &; Nadakavukaren M. J. 1977. Scanning and transmission electron microscopy of the oral sucker papillae of Philophthalmus megalurus. International Journal for Parasitology7: 429–437. Scanning electron microscopy reveals papillae on both the inside and outside of the oral sucker of the eyefluke, Philophthalmus megalurus. In the transmission electron microscope the papillae can be divided into 3 different types with 2 of these types occurring on the outside of the oral sucker. One type of outer papilla contains a bulb cell which is terminated by a cilium having an apparent typical arrangement of microtubules. This type is a presumed sensory receptor having tango- and/or rheoreceptor function. The second type of outer papilla contains a gland cell which secretes electron-dense granules to the outside of the fluke. The third type of papilla is found only on the inside of the oral sucker and contains a bulb cell terminated by a cilium which does not have the typical 9 + 2 arrangement of microtubules. Instead, their numbers increase to over 60 randomly arranged microtubules. This inner papilla is felt to have chemoreceptor function because of its location and the presence of the modified cilium. The bulb cell of the inner papilla contains 2 newly described features. The first is granular, and associated with microtubules; it may be a possible nucleating site for microtubule synthesis. The second structure is a crystalline inclusion of unknown function and origin.     

Interaction between the Effects of Inside and Outside Na and K on Bullfrog Skin Potential

The composition of the solution bathing one border of the isolated frog skin affects the response of the potential across the skin to changes in the composition of the solution bathing the opposite border. Increasing the K concentration of the inside (corium) bathing solution decreased the sensitivity of the potential to a change in outside Na concentration. Decreasing the outside Na concentration decreased the sensitivity of the potential to a change in inside K concentration. Increasing the total ionic strength of the outside bathing solution or of both bathing solutions decreased the sensitivity of the potential to a change in outside Na concentration.     

The pathways of oxalate formation from phenylalanine,tyrosine, tryptophan and ascorbic acid in the rat

The metabolic pathway by which L-[¹⁴C₁]phenylalanine, L-[¹⁴C₁]tyrosine, L-[¹⁴C₁]tryptophan, and L-[¹⁴C₁]ascorbic acid are converted to [¹⁴C]oxalate have been investigated in the male rate. Only [¹⁴C]oxalate was detected in the urine of rats injected with L-[¹⁴C₁]ascorbic acid, but [¹⁴C]-labeled oxalate, glycolate, glyoxylate, glycolaldehyde, glycine, and serine were recovered from the [¹⁴C₁]-labeled aromatic amino acids. DL-Phenyllactate, an inhibitor of glycolic acid oxidase and glycolic acid dehydrogenase, reduced the amount of [¹⁴C]oxalate recovered in the urine of rats given the [¹⁴C₁]-labeled aromatic amino acids, but increased the amount of [¹⁴C]glycolate formed from L-[¹⁴C₁]-phenylalanine and L-[¹⁴C₁]tyrosine and the amount of [¹⁴C]glycolate produced from [¹⁴C₁]tryptophan. Based on the [¹⁴C]labeled intermediates identified and the relative distribution of the radioactivity, it is postulated that phenylalanine and tyrosine are converted to oxalate via glycolate which is oxidized directly to oxalate by glycolic acid dehydrogenase. Tryptophan is metabolized via glyxylate which is oxidized directly to oxalate by glycolic acid oxidase. Neither glycolate, glyoxylate, glycolic acid oxidase or glycolic acid dehydrogenase are involved in the formation of oxalate from ascorbic acid.     

The anaerobic decomposition of benzoic acid during methane fermentation

Anaerobic rupture of the benzoic acid ring was investigated. Carbon 4 was converted primarily to carbon dioxide. Following ring rupture during methane fermentation, propanoic acid is an intermediate, and carbon 4 of benzoate becomes its carboxyl.Contribution No. 1285-j, Division of Biology, Kansas State University, Manhattan, KS 66506. This work was supported in part by funds from the Kansas Agricultural Experiment Station, Kansas State University, Manhattan, KS 66506. Paper II of this series is Fina and Fiskin (1960)