Oxidative degradation of rat mast-cell heparin proteoglycan
نویسندگان
چکیده
منابع مشابه
Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan.
Rat peritoneal mast cells were shown to inactivate thrombin rapidly. The thrombin-inactivating activity was purified to homogeneity by a combination of anion-exchange chromatography and h.p.l.c. on a Superdex 75 column. The purified thrombin inactivator had an apparent molecular mass of 29 kDa and an N-terminal amino acid sequence identical to rat mast-cell protease 1 (RMCP-1). After labelling ...
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Heparin proteoglycan formed by incubation of purified rat peritoneal mast cells with [3KS]sulfate has previously been shown to be a proteoglycan with an approximate average molecular weight of 750,000 by gel filtration. This proteoglycan which was isolated in the absence of proteases has now been shown to contain approximately equal amounts of serine and glycine which together account for 82% o...
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From the Laboratory of Clinical Znuestigation, National Institute of Allergy and Infectious Diseases, National Znstitutes of Health, Bethesda, Maryland 20205, Department of Immunology, Faculty of Medicine, Technion-lsrael Institute of Technology, P.O.B. 9649, Haifa, Israel, and Connective Tissue-Aging Research Laboratory, Veterans Administration Outpatient Clinic, Boston, Massachusetts 02108, a...
متن کاملLactoferrin regulates the activity of heparin proteoglycan-bound mast cell chymase: characterization of the binding of heparin to lactoferrin.
Rat mast cell protease 1 (RMCP-1) is a secretory granule serine protease (chymase) that is recovered in vivo in a macromolecular complex with heparin proteoglycan (PG). We have previously shown that heparin activates RMCP-1 and that RMCP-1, when bound to heparin PG, is largely resistant to inhibition by a variety of macromolecular protease inhibitors. In the search for alternative mechanisms in...
متن کاملNative heparin from rat peritoneal mast cells.
[35S]Heparin was produced in vitro by incubation of rat peritoneal mast cells with [35S]sulfate and in vivo by injection of [35S]sulfate into rats. The [35S]heparin together with nonlabeled heparin in the mast cells was isolated in native form by mild methods that avoided the use of proteolytic enzymes or high alkali concentrations. The heparin had low anticoagulant activity. Incubations of mas...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1990
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2720051