A Dynamic Growth Model of Vegetative Soya Bean Plants: Model Structure and Behaviour under Varying Root Temperature and Nitrogen Concentration

A differential equation model of vegetative growth of the soyabean plant (Glycine max (L.) Merrill cv. ‘Ransom’)was developed to account for plant growth in a phytotron systemunder variation of root temperature and nitrogen concentrationin nutrient solution. The model was tested by comparing modeloutputs with data from four different experiments. Model predictionsagreed fairly well with measured plant performance over a widerange of root temperatures and over a range of nitrogen concentrationsin nutrient solution between 0.5 and 10.0 mmol in the phytotron environment. Sensitivity analyses revealedthat the model was most sensitive to changes in parameters relatingto carbohydrate concentration in the plant and nitrogen uptakerate. Key words: Glycine max (L.) Merrill, dry matter, nitrogen uptake, partitioning, photosynthesis, respiration, sensitivity analysis     

Ribulose 1, 5-bisphosphate Carboxylase/ Oxygenase Activities in Leaves of Greenhouse Roses

An enzyme assay was developed to measure the initial and Mg²⁺–CO₂activated forms of Ribulose 1,5-bisphosphate Carboxylase/Oxygenase(Rubisco) in rose leaves. The assay was verified by co-extractionof the leaflets with partially purified spinach Rubisco andthrough correlation with net photosynthetic rates of individualleaflets (r²=0.7324). Changes in activities were measured asa function of depth of leaves in the canopy for two cultivarsof greenhouse hybrid tea roses. Initial Rubisco activity declinedwith increasing canopy depth for both cultivars. The activatedform of the enzyme, however, remained constant with canopy depthfor cv. Red Success; but increased with canopy depth, then declinedafter mid-canopy in the cv. Royalty. Rubisco activities werealso measured in the cv. Red Success grown in CO₂ enriched environments(100 mm³ dm^–3) at three humidity levels. The activitieswere not significantly affected by humidity treatment. However,there was a trend for plants grown at lower humidity to havehigher activated activities. Key words: Humidity, Rubisco, Rosa ? hybrida, Royalty, Red Success     

Cell-specific fatty acylation of proteins in cultured cells of neuronal and glial origin

Distinct sets of cellular proteins were labeled with [³H]myristic and [³H]palmitic acids in primary (rat neurons and astroglia) and continuous (murine N1E-115 neuroblastoma and rat C6 glioma) cell cultures derived from the nervous system. Both soluble and membrane proteins were modified by myristate in a hydroxylamine-stable (amide) linkage, while palmitoylated proteins were esterlinked and almost exclusively membrane bound. Chain elongation of both labeled fatty acids prior to acylation was observed, but no protein amide-liked [³H]myristate originating from [³H]palmitate was detected. Fatty acylation profiles differed considerably among most of the cell lines, except for rat astroglial and glioma cells in which myristoylated proteins appeared to be almost identical based on SDS gel electrophoresis. An unidentified 47 kDa myristoylated protein was labeled to a significantly greater extent in astroglial than in glioma cells; the expression of this protein could be related to transformation or development in cells of glial origin.     

Polyunsaturated fatty acid incorporation into plasmalogens in plasma membrane of glioma cells is preceded temporally by acylation in microsomes.

Plasmalogens (1-O-alk-1'-enyl-2-acyl-sn-glycero-3-phosphoethanolamine) are major phospholipids in many tissues and cells, particularly of neural origin. Using cultured C6 glioma cells and subcellular fractions isolated on Percoll gradients we investigated selectivity for esterification of several polyunsaturated fatty acids (PUFA) in the sn-2 position of plasmalogens compared to [1-14C]hexadecanol, representative of de novo synthesis of the ether-linked sn-1 position. In whole cells at a final concentration of 105 microM PUFA, 2-4 nmol plasmalogen/mg protein was labeled in 4 h and 10-14 nmol in 24 h, representing 8-15% and 35-50%, respectively, of initial plasmalogen mass. Incorporation of label from hexadecanol was lower than PUFA incorporation (20:5(n-3) greater than 20:4(n-6) greater than 18:3(n-3) much greater than 18:2(n-6)) suggesting deacylation-reacylation at the sn-2 position. Plasmalogens accounted for 50% of total cell ethanolamine phospholipids and 75% in plasma membrane. Using a novel, improved method for extraction of subcellular fractions containing Percoll, plasma membrane also was enriched in plasmalogen relative to microsomes (107.4 +/- 5.2 vs. 40.0 +/- 2.9 nmol/mg protein). Selectivity for esterification at the sn-2 position of plasmalogens with respect to chain length and unsaturation of the fatty acyl chain was similar in both subcellular fractions and reflected that of whole cells. Labeling of plasma membrane with PUFA and fatty alcohol lagged behind that of microsomes. Chase experiments in cells prelabeled with [1-14C]18:3(n-3) for 2 h showed no significant reduction of label in plasmalogen of any subcellular fraction although accumulation of label in the microsomal fraction was slowed initially. Reduction of plasmalogen label (40-50%) did occur in microsomes and plasma membrane when cells prelabeled for 24 h were switched to chase medium with or without chase fatty acid. Our data suggest that esterification of PUFA to plasmalogen may occur at the endoplasmic reticulum with subsequent translocation to plasma membrane resulting in accumulation of relatively stable pools of plasmalogen that are not readily accessible for deacylation-reacylation exchange with newly appearing PUFA. Alternatively, deacylation-reacylation may occur in a more stable phospholipid pool within the plasma membrane but would involve a slower process than at the endoplasmic reticulum.     

A METHOD FOR ISOLATION OF CAMPYLOBACTER SPP. (JEJUNI, COLI AND LARI) FROM SHELLFISH AND THE MARINE ENVIRONMENT

A method has been developed to detect thermophilic species of Campylobacter in shellfish, marine and tributary waters, sediment and farm runoff by-products such as manure and silage. The method consists of a 48 h enrichment incubation and subcultured to selective agars. Presumptive colonies confirmed with a latex agglutination (antibodies) to common flagellar antigens of C. jejuni, C. coli and C. lardi. Over an 8 year period, West Coast estuaries (Washington, Oregon, and California) were sampled, resulting in analysis of a total of 512 samples. Results suggest that Campylobacter spp. are well distributed in the marine environment. Two enrichment broths were compared for the recovery of campylobacters from environmental samples. The method described in the Food and Drug Administration Bacteriological Analytical Manual (FDA/BAM) (1984), was compared to a modified method. Use of the modified method described here resulted in higher recovery rates of Campylobacter spp. Recoveries of campylobacters from sediment, shellfish, and water were 10,13, and 28% higher for the modified method, respectively.     

Source of an egg kairomone for Trissolcus basalis, a parasitoid of Nezara viridula

Abstract. The eggs of the southern green stink bug, Nezara viridula (L.) (Hemiptera: Pentatomidae), are successfully attacked by Trissolcus basalis (Woll.) (Hymenoptera: Scelionidae) and are recognized as hosts by a secretion applied to the egg chorion. This secretion is produced by the follicular cells in the proximal region of the ovariole of the female pentatomid and functions as an adhesive for attaching the eggs to the oviposition substrate. The adhesive and kairomone activity could be partially removed with water. This water extract elicited host recognition behaviour in T. basalis when applied to glass beads which stuck together as the extract dried. The adhesive and kairomonal activity was removed completely with acetone since acetone-washed host eggs were not recognized by T. basalis. Application of the acetone extract to glass beads stimulated ovipositional probes by T. basalis. The adhesive appeared to be composed of a mucopolysaccharide–protein complex.