Elicitation of Necrosis in Vigna unguiculata Walp. by Homogeneous Aspergillus niger Endo-Polygalacturonase and by alpha-d-Galacturonate Oligomers

Endo-polygalacturonase (PG) was purified from a commercial preparation of Aspergillus niger pectinase by means of carboxymethylcellulose chromatography, preparative isoelectric focusing, and gel permeation through Sephadex G-50. The enzyme was electrophoretically homogeneous and consisted of a single polypeptide chain with a molecular weight of 33,500. The enzyme exhibited a specific activity significantly higher than those of purified polygalacturonases from phytopathogenic fungi. Galacturonate oligomers with a degree of polymerization higher than four appeared quickly as products of the enzymic hydrolysis of Napolygalacturonate. The oligomers were later degraded to di- and monogalacturonate. The homogeneous enzyme and growing mycelium of Aspergillus niger separately elicited a necrotic response in cowpea (Vigna unguiculata Walp.) pods. Heat-inactivated PG and PG inactivated with specific antibodies did not elicit necrosis, suggesting that the catalytic activity of the enzyme is necessary for its function as an elicitor. The PG-released oligosaccharides from Vigna cell wall and the galacturonides with a degree of polymerization greater than four separately elicited necrosis, whereas di- and monogalacturonate did not.     

Relative biological effectiveness (RBE) of neutrons produced by 50 MeV deuterons and by 34, 45, 65 and 75 MeV protons

RBE of p(34) + Be, p(45) + Be, p(65), + Be, p(75) + Be and d(50) + Be neutron beams produced at the cyclotron "Cyclone" of Louvain-la-Neuve were measured. The biological criterion was the regeneration of the crypts of the intestinal mucosa (50 regenerated crypts per circumference) after abdominal irradiation in mice. Taking the p(65) + Be neutrons as reference, RBE values were found equal to 1.12, 1.07, 1.00 (Ref.), 0.96 and 1.02 respectively. These results are consistent with those published for cell lethality in vitro. However, the RBE variation is smaller than this previously obtained in the laboratory for growth inhibition in Vicia faba.     

Chromosomal location of isozyme and seed storage protein genes in Dasypyrum villosum (L.) Candargy

Summary The zymogram phenotypes of glucose-phosphate isomerase (GPI), alcohol dehydrogenase-1 (ADH-1), glutamate oxaloacetate transaminase (GOT), superoxide dismutase (SOD), lipoxygenase (LPX), esterase (EST) and the banding patterns of gliadin and glutenin seed storage proteins were determined for Triticum aestivum cv. Chinese Spring (CS), Dasypyrum villosum, the octoploid amphiploid T. aestivum cv. Chinese Spring D. villosum (CS × v) (2n=8x=56; AABBDDVV), and for five CS-D. villosum disomic addition lines. The genes Gpi-V1, Adh-V1, Got-V2, and Sod-V2 coding for GPI-1, ADH-1, GOT-2, and SOD-2 isozymes were located in D. villosum on chromosome 1V, 4V, 6V, and 7V, respectively. Genes coding for gliadin- and glutenin-like subunits are located in D. villosum chromosomes 1V. There are no direct evidence for chromosomal location of genes coding for GOT-3, EST-1 and LPX-2 isozymes. The linkage between genes coding for glutenin-like proteins and GPI-1 isozymes in chromosome 1V is evidence of homoeology between chromosome 1V and the chromosomes of homoeologous group 1 in wheat.Research supported by the National Research Council (Italy) and National Science Foundation (USA). International cooperative project, Grant No. 85.01504.06 (CNR)     

Trichodorus persicus n. sp. (Nematoda: Trichodoridae) from Iran

Trichodorus persicus n. sp. is described from the Caspian region of Iran, where it was found in woodland and orchard soil. Males of the new species usually have two ventral cervical papillae anterior to the excretory pore but posterior to the base of the onchiostyle; there are three ventromedian preanal supplements, the posterior one lying near the heads of the retracted spicules; the spicules are 51–61 m long with faint transverse striations distally. Females have two pairs of lateral body pores, large rounded sclerotized thickenings at the vulva and the vagina tapers inwards in lateral view.     

The nuclear migration signal of Xenopus laevis nucleoplasmin.

Nucleoplasmin is the most abundant protein in the nucleus of Xenopus laevis oocytes. Its ability to target to the nucleus when microinjected into the cytoplasm has been the subject of many studies central to our understanding of how proteins segregate into nuclei. Using a cDNA clone we constructed beta-galactosidase-nucleoplasmin hybrids in modified bacterial expression vectors. The fusion proteins were expressed in Escherichia coli, purified and injected into the cytoplasm of X. laevis oocytes. The distribution of the fusion proteins between the cytoplasmic and nuclear compartments were analysed after incubation of various lengths of time. The results show that the signal sequence for nuclear transport is located close to the carboxy terminus of the protein. The signal sequence has been mapped to a small stretch of amino acids, containing a stretch of four lysines analogous to the SV40 large-T antigen signal.     

Chemical, immunological and biological properties of peptides like vasoactive-intestinal-peptide and peptide-histidine-isoleucinamide extracted from the venom of two lizards (Heloderma horridum and Heloderma suspectum)

Having previously isolated helodermin, the major peptide like vasoactive-intestinal-peptide and peptide-histidine-isoleucinamide, from the venom of the lizard Heloderma suspectum, we decided on a systematic exploration of all (VIP-PHI)-like peptides present in the venom of another lizard of the Helodermatidae family: Heloderma horridum. Six (VIP-PHI)-like peptides (PHH1 to 6) were purified to homogeneity from the venom of the lizard H. horridum with PHH3 and PHH4 representing two minor forms. All peptides cross-reacted in radioimmunoassays for helodermin and PHI but not for VIP. They yielded four fragments (T1 to T4) after trypsin digestion. T1, T2 and T3 showed the same retention time by reverse-phase HPLC and the same amino acid composition; the differences were confined to T4, the C-terminal sequence. PHH5 and PHH6 were found to be identical to synthetic helospectins I and II respectively. PHH1 and PHH3 probably resulted from a secondary modification of PHH5, while PHH2 and PHH4 derived from PHH6. Thus, the VIP-like peptides, previously called helospectins, are in fact typical of H. horridum venom. We confirmed that helodermin is the major (VIP-PHI)-like peptide of the venom of H. suspectum and observed its absence in H. horridum venom. Also, we found that positions 8 and 9 of helodermin are occupied by two Glu residues instead of two Gln as previously published. Helospectin-like material was also present in H. suspectum venom but in very small amount. In both venoms all VIP-like peptides were equally potent and efficient when tested for (a) their ability to occupy VIP as well as secretin receptors in rat pancreatic membranes and VIP receptors in rat liver membranes, and (b) the ensuing activation of adenylate cyclase in both membrane preparations.     

Contributions to the knowledge of African rotifers: Rotifers from Mauritania (W.-Africa)

The number of Rotifer taxa known from Mauritania, is raised from 8 to 90. 61% of these are cosmopolitan, 1 is temperate — boreal, 18% are thermophilic and 20% are tropicopolitan. Most of them are widely distributed in Africa, but some species have limited distributions. The presence of Keratella testudo and Wolga spinifera is remarkable and is probably related to the unusual climatic conditions in the SW Sahara. One phenotype or forma is new to science.