Morphological variation among widely dispersed larval populations of anadromous southern hemisphere lampreys (Geotriidae and Mordaciidae)

Larvae of all three southern hemisphere anadromous parasitic lampreys were collected from rivers in Australia, New Zealand and South America. Body intervals were measured, trunk myomeres counted and the frequency of pigmentation in different body regions recorded. Morphometric data were subjected to multiple group principal components analysis (MGPCA) which took into account changes during growth. The components (together with myomere counts) and the pigmentation data were both subjected to discriminant analysis. Ordination and rank correlation tests revealed no evidence for either latitudinal clines or a continuum of circumpolar change amongst larval lamprey populations. Clustering of population centroids clearly distinguished between Mordacia lapicida (Gray) from Chile and M. mordax (Richardson) from south-eastern Australia. Populations of Geotria australis Gray divided into groups representing three geographical regions, namely Argentina, Chile and Australasia (Western Australia, Tasmania and New Zealand). Ammocoetes from Argentina were the most divergent, possessing a more posterior cloaca, taller dorsal fins, a greater gap between dorsal fins, and distinctive pigmentation on the head and caudal fin. Within the Australasian group, Western Australian and New Zealand populations clustered closer than either did with those from Tasmania. The cluster analyses for larval populations of G. australis suggest that, during their marine trophic phase, the adults of this species originating from Argentinian and Chilean rivers follow different migratory routes, whereas those from Western Australia, New Zealand and, to a lesser extent, Tasmania intermix.     

Discontinuous polyacrylamide gel electrophoresis of cell wall proteinase from variants of Streptococcus lactis

An electrophoretic procedure has been developed for the separation of plasmid-coded cell wall proteinases from Streptococcus lactis NCDO strain 712. The pH and casein concentration within the electrophoresis rod during detection is more closely defined than in existing methods. The incubation conditions used with casein, (approximately pH 7 and 30dEC) may be suitable for the detection of a wider range of proteinases from other sources. Four proteinase bands present in the cell wall have been detected in milk grown cells, but only two in those previously grown in a broth medium. No cell wall proteinases were detected in a proteinase deficient variant.     

Characterization of a Neutral Aminoacyl-Peptide Hydrolase from Naegleria fowleri1

An intracellular alpha-aminoacyl-peptide hydrolase (EC 3.4.11.-) from Naegleria fowteri nN68 (ATCC 30894) has been characterized. The enzyme preparation hydrolyzed phenylalanyl-, tyrosyl-, leucyl-, arginyl-, alanyl-, tryptophanyl-, histidyl-, methionyl-, and lysyl-naphthylamide but not benzoylleucyl-, leucylglycyl-, glycylprolylleucyl-, glycyl-, threonyl-, aspartyl-, or glutamyl-naphthylamide. The aminopeptidase activity was inhibited by the cysteine-protease inhibitors—hydroxymercuribenzoate, chloromercurisulfate, and iodoacetate- by the aminopeptidase inhibitors-bestatin and trans-epoxysuccinyl-leucyl-agmatine- by an inhibitor of soluble alanyl aminopeptidase EC 3.4.11.14, puromycin, and by the metalloprotease inhibitor, o-phenanthroline. The exopeptidase activity was not inhibited by the chelator, ethylenediaminetetraacetate, or the serine-protease inhibitor, phenylmethylsulfonylfluoride. The pH optimum of the exopeptidase was between 7.0 and 8.0. Enzyme activity was stable at 55°C for 30 min, but all activity was lost after 15 min at 80°C. Enzyme activity was inhibited by 100 μM HgCI₂ and CdCl₂ but not by 1 mM CoCl₂, CuCl₂, MnCl₂, NiCl₂, FeCl₂, or ZnCl₂. Enzyme activity was inhibited by 0.1% sodium dodecyl sulfate but not by 0.2% Brij 35, Tween 20, Tween 80, or Triton X-100.     

Action of Angiotensins and Synthetic Renin Substrate on Isolated Rat Colon

AIKEN and Vane have reported¹ the independent actions of angiotensin I (AI) and angiotensin II (AII) on various isolated smooth muscle preparations, including rat colon. Tney showed that the apparent contractile action of AI on these preparations depended primarily on its in situ conversion to All by “converting enzyme” and that when the activity of the enzyme was inhibited by a pentapeptide extracted from Bothrops jararaca venom, the residual contractile action, probably due to unchanged AI, was very small. I have investigated the action of synthetic tetradecapeptide renin substrates (TPRS) on rat colon, in the light of the known actions of AI and All.     

Chloride Electrochemical Potentials and Membrane Resistances in Nitella translucens

The chloride electrochemical potential difference between theinside of cells of Nitella translucens and the bathing mediumhas been measured by a direct electrical method employing Ag/AgClelectrodes. The membrane potential has been measured by meansof conventional salt bridge microelectrodes. These data havebeen used to calculate the internal chloride concentration ofthe cells; the mean value obtained was 39 mM. This chlorideelectrochemical potential difference has been short-circuitedthus causing an outward (depolarizing) electric current to flowthrough the cell membrane. The resulting membrane depolarizationhas been measured at two points along the length of the cellenabling the membrane resistance and space constant to be deduced;the respective values obtained were 24.8 Kcm² and 3.0 cm. Itis suggested that these experiments lend additional supportto the hypothesis that during the action potential in the Characeaethere occurs a transient increase in the chloride conductanceof the plasmalemma.