Showing papers on "Holothuria published in 1987"
TL;DR: The Holothuria polii coelomocyte lysate contains two trypsin-resistant lytic proteins having different chemico-physical properties: a calcium dependent and heat-labile hemolysin and the sphingomyelin, which seems to be the membrane receptor with which both hemolysins interact producing lysis.
Abstract: The Holothuria polii coelomocyte lysate contains two trypsin-resistant lytic proteins having different chemico-physical properties : a calcium dependent and heat-labile hemolysin that is probably a constitutive component of the coelomic fluid, and another calcium independent and heat-stable one that is released after immunological stimulation; it is therefore not detectable in natural conditions. The sphingomyelin seems to be the membrane receptor with which both hemolysins interact producing lysis.
24 citations
TL;DR: The hemolytic activity of coelomic fluid from Holothuria polii is specifically inhibited by sphingomyelin and this phospholipid is the constituent of the membrane which probably interacts with the hemolysin thereby leading to the lysis.
Abstract: The hemolytic activity of coelomic fluid from Holothuria polii is specifically inhibited by sphingomyelin. This phospholipid is the constituent of the membrane which probably interacts with the hemolysin thereby leading to the lysis.
24 citations
TL;DR: It was found that the hemolytic activity of the coelomic fluid of Paracentrotus lividus against vertebrate erythrocytes corresponds to a thermo‐labile, calcinum‐dependent protein.
Abstract: The hemolytic activity of the coelomic fluid of Paracentrotus lividus against vertebrate erythrocytes was investigated. It was found that this activity corresponds to a thermo‐labile, calcinum‐dependent protein. The chemico‐physical and biological properties of this protein are compared to those of the counterparts in other echinoderm hemolytic systems. No immunological cross‐reaction could be demonstrated between P. lividus and Holothuria polii hemolysin.
15 citations