Ionic modulation of the effects of heparin and 6-aminohexanoic acid on plasminogen activation by streptokinase: The role of ionic strength, divalent cations and chloride

2003 ◽  
Vol 28 (2) ◽  
pp. 161-166 ◽  
Author(s):  
L. Guinn ◽  
J. Johnson ◽  
V. M. Doctor
1977 ◽  
Vol 55 (9) ◽  
pp. 928-934 ◽  
Author(s):  
Robert J. Maloney ◽  
David T. Dennis

A divalent cation electrode was used to measure the stability constants (association constants) for the magnesium and manganese complexes of the substrates for the NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) from pea stems. At an ionic strength of 26.5 mM and at pH 7.4 the stability constants for the Mg2+–isocitrate and Mg2+–NADP+ complexes were 0.85 ± 0.2 and 0.43 ± 0.04 mM−1 respectively and for the Mn2+–isocitrate and Mn2+–NADP+ complexes they were 1.25 ± 0.07 and 0.75 ± 0.09 mM−1 respectively. At the same ionic strength but at pH 6.0 the Mg2+–NADPH and Mn2+–NADPH complexes had stability constants of 0.95 ± 0.23 and 1.79 ± 0.34 mM−1 respectively. Oxalosuccinate and α-ketoglutarate do not form measureable complexes under these conditions. Saturation kinetics of the enzyme with respect to isocitrate and metal ions are consistent with the metal–isocitrate complex being the substrate for the enzyme. NADP+ binds to the enzyme in the free form. Saturation kinetics of NADPH and Mn2+ indicate that the metal–NADPH complex is the substrate in the reverse reaction. In contrast the pig heart enzyme appears to bind free NADPH and Mn2+. A scheme for the reaction mechanism is presented and the difference between the reversibility of the NAD+ and NADP+ enzyme is discussed in relation to the stability of the NADH and NADPH metal complexes.


1970 ◽  
Vol 45 (3) ◽  
pp. 606-614 ◽  
Author(s):  
Joseph Bryan

The characteristics of the reconstitution of a crystalline component of the sea urchin fertilization membrane are presented. The reassembly of large aggregates of cylindrical or tubular components is effected by the addition of calcium or other divalent cations. The reassembly requires a slightly alkaline pH and is little affected by increasing ionic strength. Reassembly is strongly inhibited by treatment with reducing agents such as dithiothreitol. The role of this protein in the formation of the fertilization membrane and its possible relation to the calcium-insoluble proteins of the mitotic apparatus are discussed.


1986 ◽  
Vol 14 (12) ◽  
pp. 5099-5109 ◽  
Author(s):  
Sundaram Devarajan ◽  
Richard H. Shafer

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Guang’an He ◽  
Rui Chen ◽  
Shushen Lu ◽  
Chengchun Jiang ◽  
Hong Liu ◽  
...  

Various factors affect the sedimentation behavior of nanotitanium dioxide (n-TiO2) in water. Accordingly, this study aimed to select the dominating factor. An index of sedimentation efficiency related to n-TiO2concentration was applied to precisely describe the n-TiO2sedimentation behavior. Ionic strength (IS), natural organic matter (NOM) content, and pH were evaluated in sedimentation experiments. An orthogonal experimental design was used to sequence the affecting ability of these factors. Furthermore, simulative sedimentation experiments were performed. The n-TiO2sedimentation behavior was only affected by pH and NOM content at low levels of IS. Moreover, divalent cations can efficiently influence the n-TiO2sedimentation behavior compared with monovalent cations at fixed IS. Seven different environmental water samples were also used to investigate the n-TiO2sedimentation behavior in aquatic environments. Results confirmed that IS, in which divalent cations may play an important role, was the dominating factor influencing the n-TiO2sedimentation behavior in aquatic environments.


1992 ◽  
Vol 67 (01) ◽  
pp. 111-116 ◽  
Author(s):  
Marcel Levi ◽  
Jan Paul de Boer ◽  
Dorina Roem ◽  
Jan Wouter ten Cate ◽  
C Erik Hack

SummaryInfusion of desamino-d-arginine vasopressin (DDAVP) results in an increase in plasma plasminogen activator activity. Whether this increase results in the generation of plasmin in vivo has never been established.A novel sensitive radioimmunoassay (RIA) for the measurement of the complex between plasmin and its main inhibitor α2 antiplasmin (PAP complex) was developed using monoclonal antibodies preferentially reacting with complexed and inactivated α2-antiplasmin and monoclonal antibodies against plasmin. The assay was validated in healthy volunteers and in patients with an activated fibrinolytic system.Infusion of DDAVP in a randomized placebo controlled crossover study resulted in all volunteers in a 6.6-fold increase in PAP complex, which was maximal between 15 and 30 min after the start of the infusion. Hereafter, plasma levels of PAP complex decreased with an apparent half-life of disappearance of about 120 min. Infusion of DDAVP did not induce generation of thrombin, as measured by plasma levels of prothrombin fragment F1+2 and thrombin-antithrombin III (TAT) complex.We conclude that the increase in plasminogen activator activity upon the infusion of DDAVP results in the in vivo generation of plasmin, in the absence of coagulation activation. Studying the DDAVP induced increase in PAP complex of patients with thromboembolic disease and a defective plasminogen activator response upon DDAVP may provide more insight into the role of the fibrinolytic system in the pathogenesis of thrombosis.


Langmuir ◽  
2021 ◽  
Author(s):  
Aleksandra M. Kusova ◽  
Aleksandr E. Sitnitsky ◽  
Yuriy F. Zuev
Keyword(s):  

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