Extracellular proteolytic enzymes produced by human pathogenic vibrio species

Extracellular proteolytic enzymes produced by human pathogenic vibrio species

Bacteria in the genus Vibrio produce extracellular proteolytic enzymes to obtain nutrients via digestion of various protein substrates. However, the enzymes secreted by human pathogenic species have been documented to modulate the bacterial virulence. Several species including Vibrio cholerae and V. vulnificus are known to produce thermolysin-like metalloproteases termed vibriolysin. The vibrio...

Extracellular enzymes produced by marine eukaryotes, thraustochytrids.

Extracellular enzymes produced by six strains of thraustochytrids, Thraustochytrium, Schizochytrium, and Aurantiochytrium, were investigated. These strains produced 5 to 8 kinds of the extracellular enzymes, depending on the species. Only the genus Thraustochytrium produced amylase. When insoluble cellulose was used as substrate, cellulase was not detected in the six strains of thraustochytrids...

Production of Extracellular Proteases by Human Pathogenic

Species belonging to the filamentous fungal genus Trichoderma are well known as potential candidates for the biological control of plant pathogenic fungi and as cellulase producers of biotechnological importance. Several data were published in the last decade also about the clinical importance of this genus, indicating that Trichoderma strains may be potential opportunistic pathogens of immunoc...

Exposure of fibrinogen receptor on human platelets by proteolytic enzymes.

Human platelets incubated with a-chymotrypsin or pronase did not aggregate with ADP or thrombin and did not agglutinate with ristocetin. On the other hand, they aggregated with fibrinogen even in the absence of platelet-activating compounds. This aggregation was not inhibited by prostaglandin El, sodium azide, or formaldehyde, indicating that it was independent of platelet metabolism. Calcium o...

Enhancement of reovirus infectivity by extracellular removal or alteration of the virus capsid by proteolytic enzymes.