The distribution and abundance of species of Danthonia DC on the New England Tablelands (Australia)

The distribution and percent frequency of the 13 species and one variety of Danthonia recorded on the New England Tablelands were examined in a survey of 110 predominantly pastoral sites. The relationships between site factors and the presence and percent frequency of the different Danthonia species were subjected to canonical correlation analysis. Individual species were found to have particular sets of environmental factors associated with their distribution and percent frequency; a fact not well recognized in the past. The most common factor associated with the abundance of Danthonia was either a long time since the last cultivation or no cultivation at all. Other factors such as altitude, drainage, soil parent material, soil texture and total soil phosphorus status were also of some importance. The six species most commonly recorded throughout the New England Tablelands were D. racemosa RBr, D. pilosa RBr, D. laevis J. Vickery, D. linkii Kunth., D. richardsonii Cashmore and D. tenuior (Steud.) Conert. Of these the first three are ecologically wide species. The first two can coexist with other naturalized species under grazing while D. laevis tends to disappear with disturbance. D. linkii and D. richardsonii require fairly narrow habitat conditions but these conditions and consequently these species are common. Both species respond positively to disturbance. Danthonia linkii increases with cultivation and D. richardsonii colonizes eroded soil surfaces. Danthonia tenuior has more restricted requirements and is not so frequent The other seven species and one variety did not occur often enough for detailed study and the occurrence of two of these species, D. carphoides and D. caespitosa must be considered as rare.     

Purine metabolic enzymes in lymphocytes. I. Adenosine deaminase and purine nucleoside phosphorylase activities in mouse lymphocyte subpopulations

The distribution of adenosine deaminase (ADA) and purine nucleoside phosphorylase (PNP) activities in lymphoid organs and lymphocyte subpopulations in mice, and the effect of phytohemagglutinin P (PHA-P) and concanavalin A (Con A) on the enzyme activities were studied. ADA activity was distributed equally in cells from all organs used and no mouse strain differences were observed. In contrast, PNP activity varied with the mouse strain, being highest in C57BL/6 mice and lowest in BALB/c mice, and with the organ in ICR mice, being high in peripheral blood lymphocytes and spleen lymphocytes, low in mesenteric lymph node cells and absent or very weak in thymus cells. T and B lymphocytes were prepared from spleen of ICR mice. High ADA activity was found in both T and B lymphocytes, whereas PNP activity in the T lymphocytes was about one-third of that in the B lymphocytes. PNP activity in thymus cells was increased to the normal level of T lymphocytes in the spleens by cultivation without stimulant. The development of PNP activity in thymus cells was partially inhibited by Con A but was not affected by PHA-P. ADA activity in thymus cells was enhanced by in vitro stimulation with PHA-P but not with Con A. In contrast, in spleen lymphocytes the development of ADA activity was enhanced by stimulation with PHA-P and Con A, and that of PNP activity was enhanced by PHA-P but not by Con A.     

Isozymes of Ipomoea batatas catechol oxidase differ in catalase-like activity.

The amino acid sequences of two isozymes of catechol oxidase from sweet potatoes (Ipomoea batatas) were determined by Edman degradation of BrCN cleavage fragments of the native protein and by sequencing of amplified cDNA fragments. Sequence alignment and phylogenetic analysis of plant catechol oxidases revealed about 80% equidistance between the two I. batatas catechol oxidases and approximately 40--60% to catechol oxidases of other plants. When H(2)O(2) was applied as substrate the 39 kDa isozyme, but not the 40 kDa isozyme, showed catalase-like activity. The structure of the 40 kDa isozyme was modeled on the basis of the published crystal structure of the 39 kDa isozyme [T. Klabunde et al., Nat. Struct. Biol. 5 (1998) 1084]. The active site model closely resembled that of the 39 kDa isozyme determined by crystallography, except for a mutation of Thr243 (40 kDa isozyme) to Ile241 (39 kDa isozyme) close to the dimetal center. This residue difference affects the orientation of the Glu238/236 residue, which is thought to be responsible for the catalase-like activity of the 39 kDa isozyme for which a catalytic mechanism is proposed.     

Comparative in vitro and in vivo beta-oxidation of N-nitrosodiethanolamine in different animal species

The metabolism of N-nitrosodiethanolamine (NDELA) was studied to assess whether the formation of the beta-oxidated metabolites N-(2-hydroxyethyl)-N-(formylmethyl)nitrosamine (EFMN) and N-(2-hydroxyethyl)-N-(carboxymethyl)nitrosamine (ECMN) is involved in the mechanism of tumor induction in various animal species with different susceptibility to NDELA carcinogenicity. In vitro studies using liver S9 fractions from rats, hamster, B6C3F1 and CD-1 mice and rabbits showed that all the animal species metabolize NDELA through the beta-oxidation pathway, although to different extents. Urinary excretion of NDELA and its metabolite ECMN in rats, hamsters and mice after 5 mg X kg-1 NDELA i.p. confirmed these findings. The results suggest there is no correlation between carcinogenesis by NDELA and its beta-oxidation. The possibility that ECMN formation might represent a detoxifying metabolic pathway for NDELA is discussed.     

Effect of adrenaline, glucagon and insulin on glucose metabolism in carp: influence of temperature]

In carps living since 4 months at 6, 20 or 30 degrees C, epinephrine or glucagon injections produce increase in plasma glucose but affect only slightly liver glycogen: lower is the temperature, slower and longer are the effect. Insulin injection induces more or less delayed hypoglycaemia according to temperature acclimatization; decrease in blood glucose is accompanied by a slight increase of glycogen in all tissues at 6 degrees C and on the contrary by a very strong depletion of this polysaccharide in liver and even heart at 20 and 30 degrees C.