Zobrazeno 1 - 10
of 309
pro vyhledávání: '"I H, LEPOW"'
Autor:
I H Lepow
Publikováno v:
The Journal of Immunology. 125:471-475
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::46c606139aef06d78505a7331a09fedb
https://doi.org/10.4049/jimmunol.125.2.471
https://doi.org/10.4049/jimmunol.125.2.471
Autor:
I H Lepow, J Chapitis
Publikováno v:
The Journal of Experimental Medicine
Normal human serum subjected to sucrose density gradient analysis exhibited multiple sedimenting species of properdin antigen. Properdin antigen distribution was dependent on serum concentration, ionic strength, temperature, and the presence of C3, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60640f22f75b2ccd719272d4c1327e0f
https://doi.org/10.1084/jem.143.2.241
https://doi.org/10.1084/jem.143.2.241
Publikováno v:
The Journal of Immunology. 113:1744-1751
As shown earlier, zymosan particles incubated with human citrated plasma develop the ability to induce a release reaction in platelets. Thus when incubated zymosan is shaken for 4 to 15 min with human citrated platelet-rich plasma, ADP, ATP, and 14C-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fe280be66ae46fce589fa2d7ae0151f7
https://doi.org/10.4049/jimmunol.113.6.1744
https://doi.org/10.4049/jimmunol.113.6.1744
Publikováno v:
Experimental Biology and Medicine. 145:952-957
SummaryGranule enzymes were obtained from human peripheral blood leukocytes and added to HeLa cells growing as monolayers. The enzymes disrupted the monolayer, releasing the HeLa cells, but the released cells remained vital as determined by five sepa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e09f0af7b5dd0beff1fd5947d372fd9
https://doi.org/10.3181/00379727-145-37931
https://doi.org/10.3181/00379727-145-37931
Publikováno v:
The Journal of Immunology. 110:1003-1009
Proteinases derived from Serratia marcescens and group A, β-hemolytic Streptococcus are each able to generate, by cleavage, leukotactic fragments from human C3 and C5. In whole human serum, the Serratia enzyme produces a C3-related leukotactic facto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ccfc8741515ff4a05adf9863d38438d0
https://doi.org/10.4049/jimmunol.110.4.1003
https://doi.org/10.4049/jimmunol.110.4.1003
Publikováno v:
The Journal of Immunology. 71:339-345
Summary Heat-labile factors, resembling C′1 and C′2, and a hydrazine-sensitive factor resembling C′4 are required for the inactivation of C′3 by zymosan. Certain similarities exist between the interaction of C′ with zymosan and with sensiti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed27bcf6bb68e91fe02ee145f88349ac
https://doi.org/10.4049/jimmunol.71.5.339
https://doi.org/10.4049/jimmunol.71.5.339
Publikováno v:
The Journal of Immunology. 71:331-338
Summary Mg++ is required for the inactivation of C′3 by insoluble residues of yeast cells (zymosan). The concentration of Mg++ in normal serum is more than adequate for the reaction to proceed optimally. The requirement for Mg++ is also demonstrate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0321dc80e29b7b5e130fcb6ac8b49dd
https://doi.org/10.4049/jimmunol.71.5.331
https://doi.org/10.4049/jimmunol.71.5.331
Publikováno v:
American heart journal. 93(5)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::97a70addf11fd085f970a68fc66f71e7
https://pubmed.ncbi.nlm.nih.gov/851064
https://pubmed.ncbi.nlm.nih.gov/851064
Publikováno v:
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.). 150(3)
Purified streptococcal proteinase and Serratia proteinase are potent permeability factors in rat skin and initiate histopathological evidence of an acute inflammatory response. These effects appear to be largely independent of terminal components of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4c1f8f43f38ec46018b08eca424598f
https://pubmed.ncbi.nlm.nih.gov/1798
https://pubmed.ncbi.nlm.nih.gov/1798
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 116(6)
Limited proteolysis of the third component of human complement (C3) was performed by using trypsin and streptococcal proteinase and the digests were analyzed for biologic activity. Incubation of C3 with trypsin for 1 min yielded a peptide with smooth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::24f24ea687d54979e6897371b379c222
https://pubmed.ncbi.nlm.nih.gov/774990
https://pubmed.ncbi.nlm.nih.gov/774990