Accumulation of Cyanophycin Granules as a Result of Phosphate Limitation in Agmenellum quadruplicatum

Phosphate-limited growth of the blue-green alga Agmenellum quadruplicatum resulted in the accumulation of cyanophycin granule polypeptide (CGP), which is a 1:1 co-polymer of aspartic acid and arginine. The progressive accumulation of CGP began after depletion of phosphate from the medium. CGP increased in concentration much faster than the increase in cell number. Electron microscopy indicated that both the number of cyanophycin granules per cell section and the diameter of each granule increased as phosphate starvation progressed. A marked decrease in the electron density of the inter-thylakoidal areas took place concurrently with the accumulation of CGP. At the same time a progessive decrease in the pigment concentration of cells and in the rate of nitrate uptake was observed. Thirty-two hours after phosphate depletion from the medium up to 28% of total cellular nitrogen was found in CGP.     

Individual and social behavior in a captive troop of mandrills (mandrillus sphinx)

Little is known about the behavior of mandrills in the wild, and few captive studies have been conducted. Individual and social behaviors of six captive mandrills were categorized and quantified. The captive troop consisted of one adult male, two adult females and three infants. Behavioral categories were constructed during 150 hr of preliminary observations. One hundred and sixty-seven hours of quantitative data were collected over an eight-month period. Although much of the mandrill's behavioral repertoire is similar toPapio, some facial expressions, body postures and various social behaviors were found to be unique.     

THE PRODUCTION OF HYDROGEN PEROXIDE BY BLUE-GREEN ALGAE: A SURVEY1

A survey of 38 axenic isolates of blue-green algae indicated that over half the isolates produced hydrogen peroxide under defined growth conditions. Three kinetic profiles for the formation of hydrogen peroxide, were observed; these are described. The possible site or sites of hydrogen peroxide formation remain unknown.     

Studies on the interaction of homologues of spermine with deoxyribonucleic acid and with bacterial protoplasts

Four homologues of the naturally occurring polyamine spermine, of the type H(2)N.[CH(2)](3).NH.[CH(2)] (n).NH.[CH(2)](3).NH(2) where n=2, 3, 5 and 6, have been synthesized. Their ability to stabilize Escherichia coli protoplasts against osmotic lysis was compared with that of spermine. All homologues were approximately as effective as spermine. The effect of low concentrations of the homologues on the T(m) of calf thymus DNA and of Aerobacter aerogenes DNA in 0.03m-sodium chloride-1mm-potassium dimethylglutarate buffer, pH6.2, was tested. The increase in T(m) for a given concentration of amine was found to be n=5>n=4 and n=6> n=3>n=2. When calf thymus DNA in 0.15m-sodium chloride-15mm-sodium citrate was used spermine gave the highest increase in T(m). It is concluded that the stabilization of E. coli protoplasts by tetra-amines is a non-specific effect independent of chain length, whereas the elevation of T(m) of DNA is a more specific effect which depends on chain length.     

Learning and perception of oddity problems by lemurs and seven species of monkey

Eight nonhuman primate species were compared in three experiments utilizing the oddity paradigm. The sample included 4 lemurs (Lemur catta), 26 Old World Monkeys (Macaca mulatta, M. nemestrina, M. speciosa, andCercopithecus nictitans) and 21 New World Monkeys (Cebus apella, Lagothrix humboldti andSaimiri sciurea). EveryS was first trained 60 days on “outside oddity” problems. Next,Ss solved “outside” oddity problems constituted from two short and two tall cylinders, and were tested for their perception of oddity withDavis andMcDonald's (1962) technique of varying the height of the centerplaced but nonreinforced stimulus. In the final experiment,Ss were given ambiguous oddity problems that could be solved either for form or color cues, andEs recorded preference. Cebus and woolly monkeys formed oddity learning sets as well as or better than any of the Macaque monkeys, but relatively poor performances were made by squirrel monkeys, spotnose monkeys, and lemurs. Woolly monkeys were outstandingly accurate in their perception of oddity based on changing stimulus height, no other species approaching them in this skill. Old World Monkeys were much more likely than New World Monkeys to use color as a cue.     

Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase.

Aspartate-162 in the catalytic chain of aspartate transcarbamoylase is conserved in all of the sequences determined to date. The X-ray structure of the Escherichia coli enzyme indicates that this residue is located in a loop region (160's loop) that is near the interface between two catalytic trimers and is also close to the active site. In order to test whether this conserved residue is important for support of the internal architecture of the enzyme and/or involved in transmitting homotropic and heterotropic effects, the function of this residue was studied using a mutant version of the enzyme with an alanine at this position (Asp-162----Ala) created by site-specific mutagenesis. The Asp-162----Ala enzyme exhibits a 400-fold reduction in the maximal observed specific activity, approximately 2-fold and 10-fold decreases in the aspartate and carbamoyl phosphate concentrations at half the maximal observed specific activity respectively, a loss of homotropic cooperativity, and loss of response to the regulatory nucleotides ATP and CTP. Furthermore, equilibrium binding studies indicate that the affinity of the mutant enzyme for CTP is reduced more than 10-fold. The isolated catalytic subunit exhibits a 660-fold reduction in maximal observed specific activity compared to the wild-type catalytic subunit. The Km values for aspartate and carbamoyl phosphate for the Asp-162----Ala catalytic subunit were within 2-fold of the values observed for the wild-type catalytic subunit. Computer simulations of the energy-minimized mutant enzyme indicate that the space once occupied by the side chain of Asp-162 may be filled by other side chains, suggesting that Asp-162 is important for stabilizing the internal architecture of the wild-type enzyme.