Genetic variation for aerial dispersal behavior in the Banks grass mite

Banks grass mites, Oligonychus pratensis (Banks), exhibit a behavior that facilitates their dispersal as aerial plankton over long distances. The propensity to display this behavior and its latency varies among individual mites. Some of this variation can be attributed to genetic differences among individuals. Mother-daughter resemblance and bi-directional selection were used to estimate the genetic component of latency of the aerial dispersal behavior in a wild population collected from corn plants. Mother-daughter regression analysis suggested that up to 10% of variation in initiation of aerial dispersal behavior was attributable to an additive genetic component. Subsequent selection for shorter and longer latency resulted in significant divergence between selected lines after 9 generation, but the response was not symmetrical. Realized heritability for shorter latency was 0.09, while that for longer latency was not different from 0. This response to selection was consistent with results of the mother-daughter analysis, and the response asymmetry may explain the high variability in the mother-daughter regression. In both their natural habitat and in a corn agroecosystem, mites survive by using a succession of temporarily available hosts. Aerial dispersal behavior by Banks grass mites facilitates colonization of new hosts. The genetic basis and selection response of behavior initiating aerial dispersal is consistent with its role in mites population dynamics in this setting.     

Characterization of a monoclonal antibody to human proacrosin and its use in acrosomal status evaluation.

Among the monoclonal antibodies (MAb) selected after immunization of mice with a detergent-insoluble fraction from human spermatozoa, MAb 4D4 was found to stain in immunofluorescence the principal part of the acrosome of human spermatozoa. Acrosome reaction induced decreased and spotty 4D4 immunofluorescence staining. Immunoelectron microscopy before or after embedding revealed that the epitope defined by MAb 4D4 was sequestered in the anterior acrosomal matrix and, after the acrosome reaction, remained partly bound on matrix elements attached to the inner acrosomal membrane. Western blot analysis of sperm extracts showed that the epitope defined by MAb 4D4 was located on a 55 KD polypeptide in whole cells and on 55 and 50 KD polypeptides in non-ionic detergent fractions. Human proacrosin-enriched fraction obtained by FPLC purification exhibited several proteolytic activities against gelatin in gel enzymography: a 50 KD major band and two minor bands in the 20-30 KD area; the 50 KD polypeptide reacted with MAb 4D4 in Western blots. Furthermore, the 4D4-immunoprecipitated polypeptide from sperm extract showed that the 50 KD band exhibited proteolytic activity with an optimal pH at 8.0 that was strongly inhibited by soybean trypsin inhibitor and ZnCl2. MAb 4D4 also reacted with the acrosome of the monkey Macaca fascicularis but not with the acrosome of any of the other non-primate mammalian species examined so far. Various shape defects of the acrosomal principal region were revealed by 4D4 labeling of spermatozoa with head anomalies from infertile patients. MAb 4D4 also recognized proacrosin in paraffin-embedded human testis sections. These data make the monoclonal antiproacrosin antibody 4D4 an efficient tool for evaluation of the acrosomal status of human spermatozoa and spermatids.     

R-prime plasmids from Bradyrhizobium japonicum and Rhizobium fredii

The formation of R-prime plasmids was selected in crosses involving soybean microsymbionts with genomic Tn5 insertions and carrying plasmid pJB3JI (with one IS2) copy as donors and Escherichia coli HB101 as recipient. Whereas the parent plasmid was 60 kb, recombinant plasmids between 76 kb and 121 kb were obtained. Restriction and Southern analyses confirmed the mobilization of Tn5 on four R-primes from Bradyrhizobium japonicum I-110 and on an R-prime plasmid from Rhizobium fredii HH303. The largest R-prime plasmid was obtained from the rescue of two symbiotically defective R. fredii mutant strains that required adenosine.Non-standard abbreviation TDP transposon donor pool Scientific article number A-4728 and contribution number 7724 of the Maryland Agricultural Experiment Station     

Biology of Elodea canadensis mich. and its management in Australian irrigation systems

The seasonal growth and decline of a population of Elodea canadensis Mich. growing in an irrigation drain are described, together with some characteristics of the aquatic environment (turbidity, photosynthetically-available radiation, temperature and pH). Overwintering buds (up to 5000 m^?2) in the form of swollen dormant stem apices are produced in autumn with the onset of cold weather, remain in the mud, and grow out in the spring. In late summer vegetative reproduction also occurs when large numbers of the leafless stem portions which are capable of growing into independent plants are swept downstream from established populations. Results suggest that control measures should be applied in early summer when populations are approaching nuisance size, and again in late summer before fragmentation occurs and overwintering propagules are initiated. In irrigation channels in Australia, where draining and drying are not feasible, biomass in successfully reduced by widespread use of herbicides.     

Plasma concentrations of temazepam,a 3-hydroxy benzodiazepine,determined by electron-capture gas—liquid chromatography

A simple and sensitive high-performance liquid chromatographic assay of methotrexate (MTX) and its two active metabolites, 7-hydroxymethotrexate (7-OH-MTX) and 2,4-di-amino-N¹⁰-methylpteroic acid (APA) in plasma, saliva and urine was developed. The method involved deproteinization with acetonitrile followed by addition of isoamyl alcohol and ethyl acetate. After extraction the sample was chromatographed on a cation-exchange column and monitored at 313 nm. The retention times were 5, 7 and 9 min and detection limits 20, 10 and 5 ng/ml for 7-OH-MTX, MTX and APA, respectively. For concentrations greater than 100 ng/ml one-step deproteinization of 0.1 ml sample with 0.25 ml acetonitrile was satisfactory for sample preparation. The method has been evaluated in samples from patients and rabbits receiving MTX.