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Ethiopian plants with proven and suspected molluscicidal activity: a new approach in plant evaluation.

Using available information on the toxicity, phytochemistry, ethnomedical uses and geographic distribution of plants, potentially suitable species are identified for the control of intermediate hosts of schistosomiasis in Ethiopia's lowlands where endod (Phytolacca dodecandra) is not available. Of 46 species with moderate to high snail-killing potency, 35 are indigenous to Ethiopia. They include 12 plant species with molluscicidal levels similar to those of endod, four of which are particularly suitable for snail control because of their low mammalian toxicity. Another 127 species indigenous to Ethiopia belong to genera with proven molluscicidal activity. The model for plant screening used here permits preliminary assessment of the suitability of plant resources in a given region or locality for snail control programs using existing data, without prior testing of local plants, making this approach appropriate for many developing countries.

Animals↗

The complete amino acid sequence of barley trypsin inhibitor.

The amino acid sequence of barley trypsin inhibitor has been determined. The protein is a single polypeptide consisting of 121 amino acid residues and has Mr = 13,305. No free sulfhydryl groups were detected by Ellman's reagent, which indicates the presence of five disulfide bridges in the molecule. The primary site of interaction with trypsin was tentatively assigned to the arginyl-leucyl residues at positions 33 and 34. On comparison of the sequence of this inhibitor with those of other proteinase inhibitors, we found that the barley trypsin inhibitor could not be classified into any of the established families of proteinase inhibitors (Laskowski, M., Jr., and Kato, I. (1980) Annu. Rev. Biochem. 49, 593-626) and that this inhibitor should represent a new inhibitor family. On the other hand, this trypsin inhibitor showed a considerable similarity to wheat alpha-amylase inhibitor (Kashlan, N., and Richardson, M. (1981) Phytochemistry (Oxf.) 20, 1781-1784) throughout the whole sequence, suggesting a common ancestry for both proteins. This is the first case of a possible evolutionary relationship between two inhibitors directed to totally different enzymes, a proteinase and a glycosidase.

Amino Acid Sequence↗

Lysine tRNAs from cytoplasm, chloroplasts and mitochondria of the lupin seedling cotyledons.

1. The lupin cotyledons contain two cytoplasm-specific lysine tRNAs, one chloroplast-specific, one mitochondria-specific species, and three species common to all the cell compartments investigated; the lysine tRNAs were separated by reversed-phase chromatography (RPC-5). 2. The two cytoplasmic lysine tRNAs are predominant in the tRNALys isolated from the whole tissue. Their level and relative ratios change during germination (Augustyniak & Pawełkiewicz, 1978, Phytochemistry, 17, 15-18). 3. The organellar tRNA constitutes about 20% of the total tRNA in the cotyledons of 7-day-old lupin seedlings.

Amino Acyl-tRNA Synthetases↗