In vitro studies on the binding of cloprednol to human plasma proteins

Steady-state gel filtration has been used to study the binding of cortisol to human plasma proteins in vitro. Raising the temperature from 37°C to 41°C results in the mean proportion of free (non-protein-bound) cortisol rising approximately from 7% to 11%. Addition of cortisol to plasma ≡ 275 nmol/l) also increased the proportion of free cortisol by approximately 50%. Cortisone is less strongly bound to plasma proteins than cortisol. The mean values (±S.D.) for five samples were free cortisol 8.4 ± 1.1% and free cortisone 26.0±3.8%.

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Factors affecting the stability of tPA and PAI-1 during storage and handling of human plasma for in vitro studies

Blood Coagulation & Fibrinolysis ◽

10.1097/00001721-199010000-00007 ◽

1990 ◽

Vol 1 (5) ◽

pp. 393-400 ◽

Cited By ~ 1

Author(s):

F. Hamon ◽

C. Masson-Lunven ◽

B. Boutiere ◽

C. Boyer-Neumann ◽

M. J. Larri??u ◽

...

Keyword(s):

Human Plasma ◽

In Vitro Studies ◽

Factors Affecting ◽

The Stability ◽

Pai 1

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PRESERVATION OF NORMAL HUMAN PLASMA IN THE LIQUID STATE. II. COMPARATIVE IN VITRO STUDIES ON THE PHYSIOLOGIC ACTIVITY OF LABILE CONSTITUENTS OF LIQUID AND FROZEN PLASMA 12

Journal of Clinical Investigation ◽

10.1172/jci101501 ◽

1944 ◽

Vol 23 (3) ◽

pp. 351-356 ◽

Cited By ~ 10

Author(s):

F. H. L. Taylor ◽

Eugene L. Lozner ◽

C. S. Davidson ◽

H. J. Tagnon ◽

Lloyd R. Newhouser ◽

...

Keyword(s):

Human Plasma ◽

Liquid State ◽

In Vitro Studies ◽

Normal Human Plasma ◽

Normal Human ◽

Physiologic Activity ◽

Frozen Plasma

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Chemoprotection byd-methionine against cisplatin-induced side-effects: insight from in vitro studies using human plasma

Metallomics ◽

10.1039/c3mt00238a ◽

2014 ◽

Vol 6 (3) ◽

pp. 532-541 ◽

Cited By ~ 18

Author(s):

Melani Sooriyaarachchi ◽

Wade M. White ◽

Aru Narendran ◽

Jürgen Gailer

Keyword(s):

Side Effects ◽

Human Plasma ◽

In Vitro Studies

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In Vitro Studies on Thrombolysis with Plasminogen and Streptokinase

10.1055/s-0039-1689134 ◽

1975 ◽

Author(s):

Lory R. Rice ◽

S. Sogar ◽

V. V. Kakkar

Keyword(s):

Plasminogen Activator ◽

Plasma Proteins ◽

Basic Structure ◽

In Vitro Studies ◽

Perfusion Fluid ◽

Clinical Therapy ◽

Initial Perfusion

It has been suggested that in vivo thrombi and emboli become deficient in intrinsic plasminogen (Pig) though plasma proteins are still able to percolate through the fibrin mesh which forms the basic structure of the clot. Thus it is reasonable to expect that such Pig-deficient thrombi will be degraded at a faster rate, if perfusion with a plasminogen activator is preceded by a preliminary perfusion of plasminogen itself. Such a hypothesis has important implications for clinical therapy.Our studies were undertaken in vitro, using human thrombo-emboli removed at postmortem. An initial perfusion wit 125I-labelled Pig showed an uptake of Pig into the thrombus about 3 times higher than the perfusion fluid, as shown previously (Strachan et al., 1974). Subsequent perfusion with buffer containing streptokinase (Sk) showed increased lysis under certain conditions, compared to that when either Pig was omitted from the preliminary perfusion or Sk from the main perfusion. This enhanced lysis was shown to depend upon the Pig concentration of the perfusion fluid.Strachan, C. J. L. et al. (1974), Thrombosis Res., 4, 303.

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