Determination of Plasma Urokinase Levels by Chromogenic Assay Levels: Comparison of Levels Attained During Infusion of Tissue Culture and Urinary Source Urokinase Preparations

1979 ◽  
Author(s):  
Grant H. Barlow ◽  
Victor J. Marder

Plasma urokinase levels were determined using the chromogenic substrate L-Pyroglutamyl-glycyl-L-arginine-p-nitroanalide (KABI S2444) on plasma samples collected before, during and after Infusions of tissue culture or urinary source urokinase (J, Lab. Clin. Med. 92:721, 1978). Each patient received a 2,000 IU/lb loading dose followed by an hourly rate of 2,000 IU/lb for 12 hours. There was no correlation between plasma urokinase level and critical concentration of drug or body weight and no difference in the effects of each preparation on laboratory reflections of a lytic state, such as the whole blood euglobulln lysis time, plasminogen or fibrinogen concentration. However, the chromogenic assay of urokinase activity showed that the urinary source material achieved a significantly higher plasma blood level at two hours and disappeared more rapidly after termination of the infusion than was observed with the tissue culture material. Although both urokinase infusions achieved plasma levels in excess of that required to produce a fibrinogenolytic state, it is likely that a significantly lower concentration is sufficient to produce a lytic state and that a larger dose of tissue culture material would be required to achieve this critical plasma urokinase level.

1966 ◽  
Vol 16 (01/02) ◽  
pp. 001-017 ◽  
Author(s):  
W Berg ◽  
K Korsan-Bengtsen ◽  
J Ygge

SummaryA one-stage lysis time system containing fibrinogen, streptokinase, thrombin, and a known, small amount of plasminogen was used to determine plasminogen in plasma.The known amount of plasminogen was added to the system in order to keep the lysis times relatively short when a highly diluted plasma was tested. High dilutions of plasma were used to reduce the influence of the plasma inhibitors.The calculation of the plasminogen concentration was made on the basis of the correlation: “plasminogen = fibrinogen/lysis time” which was valid in the system. The method allowed determination of plasminogen in plasma with varying fibrinogen concentrations, as the fibrinogen concentration in plasma was considered in the calculation.The presence of “spontaneous” plasmin activity in the plasma did not influence the plasminogen determination. Estimated by this method, the plasminogen content in plasma from 32 blood donors aged 25-45 years was 13.1 ±2.4 casein u/ml. The error of a single determination was 0.3 casein u/ml. The plasminogen content in plasma, determined with the present method, is about 3-4 times higher than the content found when a caseinolytic method is used.


1965 ◽  
Vol 14 (01/02) ◽  
pp. 127-144 ◽  
Author(s):  
W Berg ◽  
K Korsan-Bengtsen ◽  
J Ygge

SummaryThe lysis time method for the determination of plasminogen has been investigated using plasminogen-free thrombin and fibrinogen preparations.The experiments have shown that the lysis of a fibrin clot is the result of two consecutive reactions: the formation of fibrin which proceeds as a first order reaction and the degradation of fibrin which proceeds as a zero order reaction. Plasminogen is activated in a separate reaction. If the rate of the fibrin formation is much greater than the rate of degradation, the lysis of the fibrin clot is approximately of zero order in fibrin. The lysis time will then be inversely proportional to the plasmin concentration and proportional to the fibrinogen concentration. In a double logaritmic system the correlation between lysis time and plasmin activity is a straight line with a slope of 135°.Plasminogen is rapidly activated with streptokinase. Maximal activation is obtained only with a certain streptokinase concentration. Higher concentrations inactivate plasmin and with lower concentrations, the maximal activity is never reached. A spontaneous inactivation is seen after about 30 minutes. With urokinase, a higher maximal plasminogen activity is obtained than with streptokinase. Urokinase in higher concentrations does not inactivate plasmin.A standard assay for determination of plasminogen by the lysis time method has been worked out and is based on these results.


2010 ◽  
Vol 7 (3) ◽  
pp. 1113-1119
Author(s):  
Baghdad Science Journal

This study on the plant of Ain –AL Bason Catharanthus roseous showed the ability of callus cells that is produced by In Vitro culture technique and transformed to the accumulated media (MS 40gm/L sucrose ,2gm/L IAA Indole acetic acid , 0.5gm/L Tryptophan) to produce Vinblastine and Vincristine compounds. Extraction, purification and quantitive determination of Vinblastine and Vincristine compounds using High performance liquid chromatography technique (HPLC)were carried out. The results showed that the highest concentration of Vinblastine and Vincristine compounds were ( 4.653,12.5 (ppm /0.5 dry Wight respectively from transformed callus cells from MS 40 gm /L sucrose , 2 gm / L NAA Naphthaline acetic acid .


1978 ◽  
Vol 24 (2) ◽  
pp. 351-353 ◽  
Author(s):  
Y Inada ◽  
H Okamoto ◽  
S Kanai ◽  
Y Tamaura

Abstract Clottable fibrinogen in human plasma was determined by measuring spectrophotometrically the increase in turbidity with time due to the fibrinogen-fibrin conversion with thrombin. From the maximal absorbance, Amax, at 450 nm obtained 2 min or less after thrombin as added to plasma, we estimated the fibrinogen concentration in plasma of normal subjects and patients. Analysis of the rate of the absorbance increase yielded the Km value, 1.6 X 10(-5) mol/liter, which closely agrees with the Km of 1.2 X 10(-5) mol/liter obtained by analysis of the fibrinopeptides released from fibrinogen.


1975 ◽  
Vol 79 (4) ◽  
pp. 447-449
Author(s):  
T. G. Terent'eva ◽  
A. B. Sokolov ◽  
A. V. Laskina ◽  
R. A. Gibadulin

1970 ◽  
Vol 16 (6) ◽  
pp. 486-494 ◽  
Author(s):  
George F Grannis

Abstract The determination of plasma fibrinogen, either as clottable protein or protein precipitable with glycine or ammonium sulfate, is evaluated in terms of principles of analysis, analytic error, normal and abnormal ranges, physiologic stability, and pathologic variability of fibrinogen concentration. The quantitative comparison of analytic error, population ranges, and individual variability should permit more precise interpretation of clinical data than previously has been possible.


1977 ◽  
Vol 23 (9) ◽  
pp. 1739-1743 ◽  
Author(s):  
S Mousli ◽  
N W Wakid

Abstract Clotting of recalcified plasma is followed by an increase in its ammonia content that lasts 4 to 6 h. This ammonia production closely parallels the increase in acid-insoluble fibrin, which is evidence that the ammonia results from the action of fibrinoligase. If the clot is removed, ammonia production stops. The initial velocity of ammonia production is directly proportional to the fibrinogen concentration in plasma. Thus the rate-limiting factor in normal shed blood is the fibrinogen concentration. A maximum of 6.4 +/- 1.5 (SD) molecules of ammonia are produced per molecule of fibrinogen. Determination of the total ammonia produced is the fastest direct method of estimating the extent of frbrin cross-linkage in whole plasma. A method is proposed for assaying fibrinoligase, based on the rate of ammonia production in the presence of casein as substrate. Normal values are 7.6 +/- 2.9 (SD) mumol/min per liter of plasma.


1996 ◽  
Vol 234 (1) ◽  
pp. 97-99
Author(s):  
Barbara Schacher ◽  
Robert Reuter ◽  
Katrin Bussell ◽  
Helmut Mett

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