ABSTRACT
The authors analyze 36 cases of malaria, mainly imported. It was noted that local cases of malaria appear against the background of an increase of the incidence of imported malaria. The authors stress the fact of defects of primary diagnosis of malaria, the possibility of vaccinated cases and pathogen carrier state. The tactics of chemoprophylaxis of malaria is discussed.
Subject(s)
Malaria/diagnosis , Adult , Animals , Female , Humans , Malaria/epidemiology , Malaria/prevention & control , Male , Middle Aged , Plasmodium vivax , Russia/epidemiologySubject(s)
Bronchitis/diagnosis , Pneumoconiosis/complications , Chronic Disease , Diagnosis, Differential , Dust/adverse effects , Humans , Male , Middle AgedABSTRACT
Three compounds have been identified as sex pheromone components produced by female fall webworm moths,Hyphantria cunea (Drury). These compounds are: (Z,Z)-9,12-octadecadienal (I), (Z,Z,Z)-9,12,15-octadecatrienal (II), and (Z,Z)-3,6-cis-9,10-epoxyheneicosadiene (III). The ratio of these compounds was approximately 5â¶6â¶13, respectively, in female tip extracts prepared from U.S.S.R, insects and approximately 1â¶8â¶21, respectively, in extracts from U.S. insects. The ratio in female effluvia trapped from U.S. insects was 1â¶6â¶27, respectively. Compound III plus either I or II is effective in eliciting upwind flight in a wind tunnel. Compounds I, II, and III are also components of the sex pheromone system of the saltmarsh caterpillar moth,Estigmene acrea (Drury).
ABSTRACT
The data are presented on fractionation of cardiac and skeletal muscle Ca2+-ATPase fragments obtained by trypsin and cyanobromide hydrolysis. Amino acid composition of Ca2+-ATPases isolated from the heart and skeletal muscles and of enzyme fragments is determined. The ionophoric properties of the intact enzyme and its fragments are studied. The low-molecular weight enzyme fragment decreases velocity and the level of Ca2+-accumulation by the vesicles of sarcoplasmic reticulum. It is suggested that an "ionphoric" fragment of muscle ATPase is able to form transmembrane Ca2+-selective channel in model lipid membranes.
