High-molecular weight kininogen. A secreted platelet protein.
نویسندگان
چکیده
منابع مشابه
Colman activated platelet and activation by a platelet calpain ( s ) High molecular weight kininogen
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متن کاملPlatelet glycoprotein Ib: a zinc-dependent binding protein for the heavy chain of high-molecular-weight kininogen.
Domains 3 and 5 of high-molecular-weight kininogen (HK) have been shown to bind to platelets in a zinc-dependent reaction. However, the platelet-binding proteins responsible for this interaction have not been identified. We have focused on the platelet-binding site for the heavy chain (domain 3), which we approached using a domain 3-derived peptide ligand and isolated binding proteins by affini...
متن کاملHigh molecular weight kininogen: localization in the unstimulated and activated platelet and activation by a platelet calpain(s).
High mol wt kininogen (HMWK), the major cofactor-substrate of the contact phase of coagulation, is contained within and secreted by platelets. Studies have been performed to localize platelet HMWK in both the unstimulated and activated platelet and to ascertain the effect of platelet enzymes on HMWK itself. On platelet subcellular fractionation, platelet HMWK was localized to alpha-granules, an...
متن کاملHigh Molecular Weight Kininogen : Localization in the Unstimulated and Activated Platelet
High mol wt kininogen (HMWK), the major cofactorsubstrate of the contact phase of coagulation, is contained within and secreted by platelets. Studies have been performed to localize platelet HMWK in both the unstimulated and activated platelet and to ascertain the effect of platelet enzymes on HMWK itself. On platelet subcellular fractionation, platelet HMWK was localized to a-granules, and pla...
متن کاملHigh-molecular-weight kininogen is a binding protein for tissue prokallikrein.
Human tissue prokallikrein, a zymogen of the kallikrein-kinin system, circulates in plasma bound to neutrophils. Because plasma kininogens contribute to the assembly of kinin-generating components on blood cells, these proteins were assessed for their ability to complex the kallikrein precursor. Using ligand blot and direct binding assays, biotinylated prokallikrein was found to bind only to hi...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 1983
ISSN: 0021-9738
DOI: 10.1172/jci110901