Zobrazeno 1 - 10
of 576
pro vyhledávání: '"RW Colman"'
Autor:
RW Colman
Publikováno v:
Physiology. 7:274-278
Aggregin, a platelet surface membrane protein required for ADP-induced shape change, aggregation, and fibrinogen binding, is distinct from the receptor coupled to adenylate cyclase. Platelet aggregation by epinephrine, thromboxane A2, and collagen re
Autor:
KD Bhoola, RW Colman, Carlos D. Figueroa, J Kaufmann, LM Henderson, W Muller Esterl, RA De La Cadena
Publikováno v:
Blood. 79:754-759
An immunocytochemical study was performed to examine the cellular localization and the subcellular distribution of kininogens in human blood cells. Kininogens were visualised using the immunogold-silver staining method and confocal scanning laser mic
Publikováno v:
Blood. 81(12)
The objective of this study was to determine the role of the kallikrein- kinin system in healthy humans after intravenous administration of either Escherichia coli endotoxin or saline. We studied a total of 18 healthy nonsmoking volunteers, 23 to 38
Publikováno v:
Blood. 77(3)
In this study we show that high molecular weight kininogen (HK) inhibited alpha-thrombin-induced aggregation of human platelets in a dose-dependent manner with complete inhibition occurring at plasma concentration (0.67 mumol/L) of HK. HK (0.67 mumol
Publikováno v:
Blood. 87:2089-2089
Publikováno v:
Blood. 53:1033-1042
Publikováno v:
Blood. 56:596-607
Human and rhesus monkey platelets secrete at least two antiheparin proteins: platelet factor 4 (PF4) and low affinity platelet factor 4 (LA-PF4). Neither of these proteins showed species-related antigenic differences. As determined by radioimmunoassa
Publikováno v:
Blood. 69:1431-1436
Human plasma kallikrein, a product of contact-activated plasma proteolysis, is moderately inhibited by aprotinin, a small polypeptide from bovine lung that has been used as an experimental drug in human disease states. Aprotinin has a Lys residue in
Publikováno v:
Blood. 70:796-803
Previous reports have indicated that the nucleotide affinity analog 5′- p-fluorosulfonylbenzoyl adenosine (FSBA) at concentrations between 40 and 100 mumol/L and at times greater than 20 minutes covalently modifies a single protein component on the
Publikováno v:
Blood. 71:388-394
Platelets are known to process human factor V during secretion and/or membrane binding. We studied the functional and structural changes produced in human factor V by purified human platelet calpain (calcium- activated thiol protease) and compared th