First report of Amblyomma latepunctatum and the second record of Ixodes luciae in the state of Acre, Brazil.

The state of Acre is in the western part of the Brazilian Amazon region and few studies involving ticks are available. The aim of the present study was to provide the first report of occurrence of Amblyomma latepunctatum and the second record of Ixodes luciae in Acre. Ticks were collected in October 2020 inside an open forested area in the municipality of Rio Branco, the state capital of Acre.

SBTX, a new toxic protein distinct from soyatoxin and other toxic soybean [Glycine max] proteins, and its inhibitory effect on Cercospora sojina growth.

SBTX, a novel toxin from soybean, was purified by ammonium sulfate fractionation followed by chromatographic steps DEAE-Cellulose, CM-Sepharose and Superdex 200 HR fast-protein liquid chromatography (FPLC). Lethality of SBTX to mice (LD(50) 5.6 mg/kg) was used as parameter in the purification steps.

Nutritional study of two Brazilian soybean (Glycine max) cultivars differing in the contents of antinutritional and toxic proteins.

The research was conducted with two different recently released Brazilian soybean cultivars (Rio Balsas and Bays) to evaluate whether there is any correlation between the different levels of antinutritional and/or toxic proteins in the cultivars and their nutritive value as sources of protein for monogastric animals (rats). Furthermore, it is discussed, for the first time, the role of the dietary soyatoxin on the performance of rats fed on diets containing soyatoxin-rich (cv. Bays) and soyatoxin-free (cv.

Purification of a novel antibacterial and haemagglutinating protein from the purple gland of the sea hare, Aplysia dactylomela rang, 1828.

Physicochemical characterisation and antibacterial and haemagglutinating properties of a new protein isolated from purple fluid of the Aplysia dactylomela are reported. The purification procedure consisted basically of ammonium sulphate fractionation, ion exchange, exclusion molecular and hydrophobic interaction chromatography. The highly purified protein, designated dactylomelin-P, is a single chain protein of 60,000 Da by SDS-polyacrylamide gel electrophoresis and 56,200 Da by gel filtration on calibrated Superose column at pH 7.