Mitochondrial degeneration after organic phosphate poisoning in prosimian primates

Summary The degenerative reaction of mitochondria to tricresylphosphate (TCP) poisoning in spinal ganglion cells of Slow Loris (Nycticebus coucang coucang) were studied with the electron microscope. In neurones of animals treated with TCP, mitochondria display various stages of alterations which confirm mitochondrial involvement in TCP poisoning. The role of degenerated mitochondria in the formation of neuronal lipofuscin is discussed. It is suggested that the lipofuscin granule is a metabolic product inherently related to mitochondrial degeneration, irrespective of the primary cause: ageing or intoxication.Fellow of the Deutscher Akademischer Austauschdienst on study leave from the Medical Faculty, University of SingaporeA grant from the Deutsche Forschungsgemeinschaft (Gl. 28/20) is gratefully acknowledgedThe skilfull technical assistance of Mr. Tajuddin b.M. Ali, Mr. P. Gopal, Mr. R. Dungan and Mrs. C. Weinrichter is gratefully acknowledged     

Biosynthesis of pterocarpan phytoalexins in Trifolium pratense

Feeding experiments have demonstrated that 7,2′-dihydroxy-4′-methoxy-isoflavone-[¹⁴C-Me] and -isoflavanone-[¹⁴C-Me] are extremely efficient precursors of the phytoalexin demethylhomopterocarpin in Cu²⁺-treated red clover seedlings. Neither of these compounds, nor demethylhomopterocarpin-[¹⁴C-Me], was incorporated into a second pterocarpan phytoalexin, maackiain. 3-Hydroxy-9-methoxypterocarp-6a-ene-[¹⁴C-Me] was a poor precursor of both pterocarpans. A biosynthetic pathway to demethylhomopterocarpin via 2′-hydroxylation of formononetin (7-hydroxy-4′-methoxyisoflavone) and subsequent reduction to the isoflavanone is proposed. The conversion of this isoflavanone into the pterocarpan may involve the corresponding isoflavanol and a carbonium ion intermediate. The branch-point to maackiain is probably at the formononetin stage. The presence of two coumestans, 9-O-methylcoumestrol and medicagol, previously unreported in red clover, is demonstrated. Biosynthetic implications are discussed.     

Long-term survey data (1965-1972) on the occurrence of Anisakis larvae (Nematoda: Ascaridida) in herring, Clupea harengus L., from the North Sea

The occurrence of larval Anisakis in North Sea herring was examined during the period 1965-1972 using a sampling method which yielded comparable data for all eight years. Data on abundance of infestation in several herring stocks pointed to remarkable fluctuations over the study period with an increase in the period 1966-1968 followed by a decrease in the period 1968-1972. Of various hypotheses that may explain this situation, it is concluded that changes in the migration behaviour of the herring may be responsible. Other data and statistics are discussed with special reference to variations in infestation level in different samples and to the occurrence of adult nematodes in marine mammals.     

Interaction of methotrexate with polycationic carriers

Binding parameters were measured for the $\text{in vitro}$ interaction of methotrexate with poly-L-lysine and diethylaminoethyl dextran. The complexes were found to have apparent affinity constants of 2590 and 440 M^?1 respectively at 37°, ionic strength 0.02. For hypotonic solutions containing therapeutic concentrations of methotrexate, this results in 87% binding of the drug to poly-L-lysine and 74% to diethylaminoethyl dextran. While the binding decreased to about 50% upon increasing ionic strength to physiologic levels, sufficient drug-carrying capacity was retained at isotonicity to support the potential utility of such complexes as tissue-specific drug carriers.     

Genetic architecture of yield and components of yield in mustard (Brassica juncea (L.) Czern & Coss.)

Summary The relative ability of cross- and self-pollen to achieve fertilisation in Brassica was studied by making double pollinations using cross-pollen carrying a dominant seedling marker gene. With simultaneous self- and crosspollination 12–40% self-seed was set, but when cross-pollen was applied to the stigma four hours before self-pollen, only 2–4% self-seed was obtained. In two plants to which cross-pollen was applied at various time intervals after self-pollen there was a tendency for the percentage of self-seed to increase as the time interval increased. In a third plant this trend was not apparent, probably because of a greater degree of self-incompatibility. The competitive advantage of the first pollen to arrive on the stigma is discussed in relation to the strength of the self-incompatibility and the sib problem in F₁ hybrid brassicas.     

Purification and properties of mammalian toxins from the venom of the Brazilian scorpion Tityus serrulatus Lutz and Mello

The water-soluble part of the dried venom from the scorpion, Tityus serrulatus Lutz and Mello (range, Southeastern Brazil), showed 16 polypeptide bands on polyacrylamide gel electrophoresis. This material exhibited toxic and hyaluronidase activity but no phospholipase, phosphodiesterase, protease, or fibrinolytic activity. Fractionation on glycinamide-treated Sephadex G-50 afforded three protein fractions, which were non-toxic, equitoxic, and three times more toxic than the water-soluble venom. Subsequent separation of the toxic fractions on carboxymethyl-cellulose with phosphate buffers furnished five toxic components, which were further purified on carboxymethyl-cellulose with a salt gradient in acetate buffer. Toxin γ, the major and most basic toxin, is a 62-residue protein that, unlike other scorpion toxins, contains methionine. Automated Edman degradation showed the amino-terminal sequence to be H-Lys-Glu-Gly-Tyr-Leu-Met-Asp-His-Glu-Gly-Cys-Lys-Leu-Ser-Cys-Phe-Ile-Arg-Pro-Ser-Gly-Tyr-Cys-Gly-Arg-Glu-Cys-Gly-Ile-. Toxin γ is the first example of a fifth structural type of mammalian toxin from scorpion venom. Its amino-terminal sequence shows greater homology with toxins similar to Centruroides suffusus suffusus toxin III and Androctonus australis toxin II than with toxins similar to A. australis toxin I or Bhutus occitanus tunetanus toxin I.