Differential scanning calorimetry of α2-macroglobulin and α2-macroglobulin-proteinase complexes
نویسندگان
چکیده
منابع مشابه
Inactivation of α2-Macroglobulin by Activated Human Polymorphonuclear Leukocytes
The proteolytic activity of trypsin releases the dye Remazol Brilliant Blue from its high molecular weight substrate, the skin powder (Hide Powder Azure, Sigma), with an increase in absorbance at 595 nm. Active alpha(2)- macroglobulin (80 mug/ml) totally inhibits the proteolytic activity of trypsin (14 mug/ml) by trapping this protease. But after a 20 min incubation of alpha(2)-macroglobulin at...
متن کاملUnique Features of a Pseudomonas aeruginosa α2-Macroglobulin Homolog
UNLABELLED Human pathogens frequently use protein mimicry to manipulate host cells in order to promote their survival. Here we show that the opportunistic pathogen Pseudomonas aeruginosa synthesizes a structural homolog of the human α2-macroglobulin, a large-spectrum protease inhibitor and important player of innate immunity. Small-angle X-ray scattering analysis demonstrated that the fold of P...
متن کاملStudies on Human Plasma Α2-macroglobulin-enzyme Interactions
Human plasma alpha(2)-macroglobulin is an inhibitor of circulating proteases that function in hemostatic and inflammatory reactions but the biochemical nature of its interaction with these enzymes is not well defined. This investigation has found that alpha(2)-macroglobulin is comprised of subunit chains of 185,000 molecular weight as analyzed by electrophoresis in polyacrylamide gels containin...
متن کاملMetabolism of the Complex Monofluorophosphate-α2-macroglobulin in the Rat
Sodium monofluorophosphate (MFP) is a drug used in the treatment of primary osteoporosis. Following the intake of MFP, a small fraction of the drug is absorbed intact and forms a complex with α2-macroglobulin (MFP-α2M) inactivating the antiproteasic activity of the globulin. The complex has been shown to occur in the serum of rats and human being. This paper reports data on the metabolism of th...
متن کاملImmunotherapy of Tumors with α2-Macroglobulin-Antigen Complexes Pre-Formed In Vivo
The cell surface receptor CD91/LRP-1 binds to immunogenic heat shock proteins (HSP) and α(2)M ligands to elicit T cell immune responses. In order to generate specific immune responses, the peptides chaperoned by HSPs or α(2)M are cross-presented on MHC molecules to T cells. While the immunogenic HSPs naturally chaperone peptides within cells and can be purified as an intact HSP-peptide complex,...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1983
ISSN: 0264-6021
DOI: 10.1042/bj2090725