The Action of Streptomycins on the Chloroplast System of Euglena gracilis

Five streptomycins bleached the chloroplast system of Euglena gracilis; the most effective were those which contained an aldehyde group in the streptose moiety: streptomycin and hydroxystreptomycin. Derivatives containing a secondary alcohol group in place of the aldehyde (dihydro-, dihydrodesoxy-, dihydrohydroxystreptomycin) require higher concentrations to elicit the same effect. Hydroxylamine reversed the bleaching effects of streptomycin and hydroxystreptomycin but not of dihydro-, dihydrodesoxy-or dihydrohydroxystreptomycin. These observations suggest that the aldehyde group of the streptomycins contributes to the action of these antibiotics on Euglena chloroplasts; the action of hydroxylamine would be to either remove the antibiotic from its site of action or to render it ineffective in vivo by reaction with the aldehyde group

A xylanase gene from Bacillus subtilis: nucleotide sequence and comparison with B. pumilus gene: Arch.Microbiol.

NRC publication: Ye

Global Health and Epilepsy: Update and Future Directions

Purpose of Review: Efforts to improve epilepsy care outcomes in low- and middle-income countries (LMICs) are occurring through global health work. Despite an increase in these efforts, several barriers exist and a significant epilepsy treatment gap remains. This paper will review barriers to epilepsy care in LMICs and summarize recent published and unpublished data about global health projects which aimed to improve epilepsy care in these regions, focusing on work in the past 5 years. Recent Findings: There are multiple recent and ongoing projects including clinical, research, education, and advocacy programs. Summary: We conclude that collaborative efforts are necessary in order to develop long-term and sustainable projects. The creation of a database and a formal method of communication between stakeholders can contribute to improving the efficiency and impact of global health efforts in epilepsy

Amino acid sequence and thermostability of xylanase A from Schizophyllum commune

The amino acid sequence (197 residues) of xylanase A from the fungus, Schizophyllum commune, was determined by automated analysis of peptides from proteolytic and acid cleavage. The sequence is similar to two Trichoderma xylanases (approximately 56% identical amino acids), but also shows at least 40% identities with xylanases from Bacillus subtilis, B. pumilus and B. circulans. The conserved regions of the enzyme contain only two glutamic acid residues which implicates their possible involvement in catalysis. The disulfide bond in xylanase A is not conserved in this family. In spite of this, the B. subtilis xylanase was found to be more thermostable than xylanase A.Peer reviewed: YesNRC publication: Ye