Magnetic Behavior of Co/Pt and TbCo Nanocaps Assembly for Bit Pattern Media

Large area patterning of self-assembled alumina nanobumps, with hexagonally close-packed order, has been used to create ordered array of bit pattern magnetic media. We have studied the magnetic properties of perpendicular magnetic TbCo alloy and Co/Pt multilayers deposited on self assembled alumina nanobumps. Measurement of reversal field as a function of field intensity, as well as magnetic force microscopy images confirm the weakness of exchange coupling between bits in the case of Co/Pt multilayer while stronger coupling is observed in the case of TbCo alloys. When you are citing the document, use the following link http://essuir.sumdu.edu.ua/handle/123456789/3535

Magnetic Behavior of Co/Pt and TbCo Nanocaps Assembly for Bit Pattern Media

Large area patterning of self-assembled alumina nanobumps, with hexagonally close-packed order, has been used to create ordered array of bit pattern magnetic media. We have studied the magnetic properties of perpendicular magnetic TbCo alloy and Co/Pt multilayers deposited on self assembled alumina nanobumps. Measurement of reversal field as a function of field intensity, as well as magnetic force microscopy images confirm the weakness of exchange coupling between bits in the case of Co/Pt multilayer while stronger coupling is observed in the case of TbCo alloys. When you are citing the document, use the following link http://essuir.sumdu.edu.ua/handle/123456789/3535

Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors

Human plasma kallikrein, a serine proteinase, plays a key role in intrinsic blood clotting, in the kallikrein-kinin system, and in fibrinolysis. The proteolytic enzymes involved in these processes are usually controlled by specific inhibitors and may be influenced by several factors including glycosaminoglycans, as recently demonstrated by our group. The aim of the present study was to investigate the effect of glycosaminoglycans (30 to 250 µg/ml) on kallikrein activity on plasminogen and factor XII and on the inhibition of kallikrein by the plasma proteins C1-inhibitor and antithrombin. Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the catalytic efficiency of kallikrein (in a nanomolar range) on the hydrolysis of plasminogen (0.3 to 1.8 µM) and increased (1.9 to 7.7 times) the enzyme efficiency in factor XII (0.1 to 10 µM) activation. On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 µM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Heparin and heparan sulfate increased (1.4 times) the enzyme inhibition by the C1-inhibitor (150 nM).Universidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de BioquímicaUniversidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de BiofísicaUNIFESP, EPM, Depto. de BioquímicaUNIFESP, EPM, Depto. de BiofísicaSciEL