Acetylene reduction by nitrogen-fixing blue-green algae

Summary Known nitrogen-fixing species of blue-green algae are capable of reducing acetylene to ethylene, but acetylene is not reduced by Anacystis nidulans, which does not fix nitrogen. Cycad root nodules which contain blue-green algae as endophytes reduce acetylene. Acetylene reduction is inhibited by carbon monoxide. Nitrate or ammonium-nitrogen has no immediate effect on algae reducing acetylene, but algae grown on nitrate-nitrogen gradually lose their capacity to reduce acetylene. Nitrate-nitrogen also inhibits heterocyst formation in these algae and there is a fairly direct correlation between the abundance of heterocysts in a particular sample and its capacity to reduce acetylene. Aphanizomenon flosaquae reduces acetylene and fixes nitrogen in unialgal culture and there is strong presumptive evidence that these reductions are carried out by the alga rather than by associated bacteria. The molar ratios of ethylene: ammonia produced vary within the range 1.4–1.8.     

Lateral phase separations and perpendicular transport in membranes

A valinomycin-mediated potassium conductivity has been studied using a glass U-tube in which two aqueous compartments are separated by a fritted glass filter impregnated with valinomycin and one or more pure phospholipids. This system can be used to detect the beginning and end of lateral phase separations in binary lipid mixtures, and also demonstrates a pronounced maximum in electrical conductivity of dipalmitoyl phosphatidylcholine at the transition temperature, 41°C.     

The existence of a second route for the transfer of certain glycoproteins from the circulation into the liver.

Oligosaccharide chains of agalactoorosomucoid, α₁-acid glycoprotein from which sialic acid and galactose have been sequentially removed, terminate in N-acetylglucosaminyl residues. This protein is rapidly transferred from the circulation into the liver by a route distinct from that previously demonstrated for a number of galactosyl terminating glycoproteins.     

Neurohormonal Integration of Osmotic and Ionic Regulation

There is evidence in crustaceans that neuroendocrine centers,including the eyestalk, brain, thoracic ganglionic mass, andpericardial organ, produce factors that affect osmotic and ionicregulation. Understanding of the processes responsible for osmoticadjustment in the intact animal, such as regulation of permeability,active uptake of ions, and respiratory and cardiovascular alterations,has increased substantially in the past few years. However,interaction of neuroendocrine factors with the target tissuesand systems is just beginning to be investigated. There is evidencethat content of lipids and activity of enzymes are importantin osmoregulation, and neuroendocrine effects on these metabolicprocesses are worthy of study. In addition, there are some crustaceansin which osmoregulatory ability varies developmentally. Furtherinvestigations of such animals is also necessary. Progress inour understanding of neuroendocrine influences on osmoregulationdepends upon further purification of active factors from neuroendocrinecenters and hemolymph, and upon development of appropriate assayson which to test them.     

Adenosine binding sites of rat pheochromocytoma PC 12 cell membranes: partial characterization and solubilization

Rat pheochromocytoma PC 12 cell membranes were shown to possess A2-like adenosine binding sites as assessed by using 5'-N-ethylcarboxamide[3H]adenosine [( 3H]NECA). Specific [3H]NECA binding to PC 12 cell membrane at 0 degrees C was saturable and showed a monophasic saturation profile. In contrast, [3H]NECA binding to PC 12 cell membrane at 30 degrees C exhibited a biphasic profile suggesting the presence of two specific binding site. The rank order of potency for inhibition of [3H]NECA binding at 0 degrees C was NECA greater than 2-chloroadenosine greater than 2',5'-dideoxyadenosine greater than isobutylmethylxanthine much greater than phenylisopropyladenosine. These adenosine binding sites were solubilized with sodium cholate and the solubilized portion retained the same ligand binding characteristics as those of the membrane-bound form. Gel filtration experiments indicated an apparent Stokes radius of 6.7 nm for these adenosine binding sites/detergent complexes.