منابع مشابه
lysosomal-enzyme release in cultured mouse calvaria
The effect of bradykinin on bone resorption was studied in cultures of newbornmouse calvaria. Bradykinin (0.03,UM, 1 Mm) stimulated the release of 4'Ca2+ from bones dissected out from mice prelabelled in vivo with 45Ca. Bradykinin (1 Mm) also augmented the release of stable calcium (4"Ca), Pi and the lysosomal enzyme f,glucuronidase. The stimulatory effect of bradykinin on mineral mobilization ...
متن کاملPRODUCTION, RELEASE AND THERMAL CHARACTERIZATION OF CELLULOLYTIC ENZYME FROM CELLULOMONAS sp. STRAIN "0"
Cellulase production by a Cellulomonas sp., isolated in 1985 from forest humus soil along the border of the Caspian Sea in Iran, was investigated. This strain secreted endo-and exo-cellulases in the culture medium, but some of the enzymes produced remained cell membrane bound. Cell bound enzymes were released by various treatments. The highest amount of endo-glucanase (up to 95%) and exo-gl...
متن کاملChanges in ionic movements across rabbit polymorphonuclear leukocyte membranes during lysosomal enzyme release. Possible ionic basis for lysosomal enzyme release
Changes in the movements of Na+, K+, and Ca+2 across rabbit neutrophils under conditions of lysosomal enzyme release have been studied. We have found that in the presence of cytochalasin B, the chemotactic factor formyl methionyl leucyl phenylalanine (FMLP) induces within 30 s large enhancements in the influxes of both 22Na+ and 45Ca+2 and an increase in the cellular pool of exchangeable calciu...
متن کاملHormone-elicited enzyme release by the small intestinal wall.
Three enzymes of intestinal origin-enterokinase, alkaline phosphatase, and sucrase-were released into the perfused small intestinal lumen of the rat upon intravenous injection of the gastrointestinal hormone cholecystokinin-pancreozymin (CCK-PZ). The presence of bile in the perfusion fluid greatly augmented this release. The results suggest that a combined mechanism of enzyme liberation due to ...
متن کاملEnzyme-triggered cargo release from methionine sulfoxide containing copolypeptide vesicles.
We have developed a facile, scalable method for preparation of enzyme-responsive copolypeptide vesicles that requires no protecting groups or expensive components. We designed amphiphilic copolypeptides containing segments of water-soluble methionine sulfoxide, M(O), residues that were prepared by synthesis of a fully hydrophobic precursor diblock copolypeptide, poly(l-methionine)65-b-poly(L-le...
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ژورنال
عنوان ژورنال: Clinical Chemistry and Laboratory Medicine
سال: 1987
ISSN: 1434-6621,1437-4331
DOI: 10.1515/cclm.1987.25.9.525