Polyacetylenes from the spongePetrosia ficiformis found in dark caves

Summary Several high molecular weight polyacetylenes have been isolated from the spongePetrosia ficiformis found in dark caves. These compounds are related to, but different from, the polyacetylenes isolated from the same sponge living in its usual habitat.This work is a part of the Progetto finalizzato per l'Oceanografia e i Fondi Marini, CNR, Roma.The authors thank Mr G. Scognamiglio for the HPLC work, Mr C. Di Pinto for the NMR spectra and Mr G. Villani for the collection of the sponge.     

Incorporation of α-aminobutyric acid into ergostine byClaviceps purpurea

Summary Claviceps purpurea 275 F.I. fed with -aminobutyric acid produces ergostine with the corresponding -hydroxy--aminoacid undiluted by endogenous aminoacid. Almost all the -aminobutyric acid not incorporated into the ergostine remains unchanged in the medium. The significance of these results in the biosynthesis of ergot alkaloids is discussed.     

Spontaneous maze ambulation in two mouse strains

Summary A simple device is described, which permits us to quantify several parameters of spontaneous behaviour of small animals. Using this device with mice we obtained statistically satisfactory results, showing a strong genetic influence on the behavioural characteristics tested.We wish to thank Mr R. Laplace for technical help, Mr J. P. Arnould for electronic work as well as I.N.S.E.R.M.-SCR 3.     

Inhibitory tripeptide,Lys-Phe-Tyr,as a fragment of physalaemin

Summary Several peptides were separated from-chymotrypsin-treated physalaemin by high voltage paper electrophoresis, and inhibition of the excitability of a molluscan giant neurone (tonically autoactive neurone) by the tripeptide, Lys-Phe-Tyr, was demonstrated.We thank Dr Sadaaki Iwanaga of Osaka University and Dr Atsuo Inoue of Daiichi Pharmaceutical CO for their helpful advice and the donation of the tripeptide (Lys-Phe-Tyr).     

Occurrence of β-chitin in the cuticle of a Pentastomid Raillietiella gowrii

Summary The purified chitin from the cuticle of a pentastomid was examined by X-ray method. The X-ray photograph discloses that the chitin in question is of -type. Since the arthropod cuticle contains -chitin, it is suggested that Pentastomida may be considered an independent phylum.Thanks are due to Prof. Dr. G. Sundara Rajulu for guidance and encouragement.     

In vivo effects of Escherichia coli endotoxin on sulfobromophthalein clearance in the guinea-pig.

In vivo studies indicated that the primary effects of E. coli endotoxin on hepatic clearance of sulfobromophthalein were at the excretory level. Newborns were more sensitive to the LPS than older animals.     

Snake venom action: Are enzymes involved in it?

Summary Enzymes were the first clearly recognized components of snake venoms. When several more were discovered, attempts were made to correlate venom action with enzymic functions. The last few years have seen most successful efforts in the identification, isolation and structural elucidation of highly toxic polypeptides present in snake venoms, in particular of neurotoxins and membrane-active toxins. Following this development the polypeptides were called the true toxic components and the enzymes lost their previous central position in venom pharmacology. The time, therefore, has come to re-evaluate the role of enzymes in the complex interaction between snake and prey. While highly active polypeptides indeed dominate the action of hydrophiid venoms, they appear to play a lesser role in crotalid venom action as compared with enzyme components. Enzymes are involved in many levels of venom action, e. g. by serving as spreading factors, of by producing very active agents, such as bradykinin and lysolecithins in tissues of preys or predators. Some toxins, e. g. the membrane-active polypeptides appear to participate in the interaction between membrane phospholipids and venom phospholipases. The classical neurotoxin, -bungarotoxin, has been recognized as a powerful phospholipase. Several instances are known which indicate that some enzymes potentiate the toxic action of others; the analysis of a single enzyme may, therefore, not fully reveal its biofunction. For 3 enzymes, ophidianl-amino acid oxidase, ATPpyrophosphatase, and acetylcholinesterase, some of the problems pertaining to venom toxicity are discussed.