Zobrazeno 1 - 5
of 5
pro vyhledávání: '"J L Sprows"'
Publikováno v:
The Journal of Immunology. 145:2652-2661
Human mast cells can be divided into two subsets based on serine proteinase composition: a subset that contains the serine proteinases tryptase and chymase (MCTC), and a subset that contains only tryptase (MCT). In this study we examined both types o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7d9d5e329fd2055638629907b24a64a9
https://doi.org/10.4049/jimmunol.145.8.2652
https://doi.org/10.4049/jimmunol.145.8.2652
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 145(8)
Human mast cells can be divided into two subsets based on serine proteinase composition: a subset that contains the serine proteinases tryptase and chymase (MCTC), and a subset that contains only tryptase (MCT). In this study we examined both types o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::998c2b0930fc0e003cdfca262cc03c6c
https://pubmed.ncbi.nlm.nih.gov/2212656
https://pubmed.ncbi.nlm.nih.gov/2212656
Autor:
Norman M. Schechter, Barry S. Cooperman, Harvey Rubin, J L Sprows, O. L. Schoenberger, Gerald S. Lazarus
Publikováno v:
Journal of Biological Chemistry. 264:21308-21315
The ability of plasma proteinase inhibitors to inactivate human chymase, a chymotrypsin-like proteinase stored within mast cell secretory granules, was investigated. Incubation with plasma resulted in over 80% inhibition of chymase hydrolytic activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f04d8d48b5e3e95dbe856adcadfdef82
https://doi.org/10.1016/s0021-9258(19)30080-8
https://doi.org/10.1016/s0021-9258(19)30080-8
Publikováno v:
The Journal of biological chemistry. 264(35)
The ability of plasma proteinase inhibitors to inactivate human chymase, a chymotrypsin-like proteinase stored within mast cell secretory granules, was investigated. Incubation with plasma resulted in over 80% inhibition of chymase hydrolytic activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2469c0f15640538e5b3d80e40d9cbd56
https://pubmed.ncbi.nlm.nih.gov/2592376
https://pubmed.ncbi.nlm.nih.gov/2592376
Publikováno v:
FEBS letters. 259(1)
Limited proteolysis of C1-inhibitor was observed with human skin chymase, human cathepsin G, and bovine chymotrypsin. In each case, the inhibitor was degraded to one major product migrating slightly faster than the native inhibitor in an SDS-polyacry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::584e1d48700342dcbd649d3349136983
https://pubmed.ncbi.nlm.nih.gov/2599103
https://pubmed.ncbi.nlm.nih.gov/2599103