Method for Determination of Cyclic AMP in Plasma

1973 ◽  
Vol 19 (3) ◽  
pp. 312-314 ◽  
Author(s):  
Babeth Rabinowitz ◽  
Joseph Katz
Keyword(s):  
Cyclic Amp ◽  
Human Plasma ◽  
Ammonium Sulfate ◽  
Protein Complex ◽  
Clinical Studies ◽  
Simple Procedure ◽  
Normal Human Plasma ◽  
Tissue Extracts ◽  
Normal Human

Abstract A simple procedure is described for measuring cyclic AMP (cAMP) in plasma, body fluids, and tissue extracts. A modification of the method of Brown et al. [Biochem. J. 121, 561 (1971)], it is based on competitive binding of cAMP by a protein in crude adrenal extracts, and precipitation of the cAMP-protein complex by ammonium sulfate. cAMP concentrations in normal human plasma ranged from 8 to 16 nmol/liter, and in the plasma of dogs from 5 to 15 nmol/liter. The range of the method is 0.5-8 pmol per assay, and up to 0.4 ml of sample can be used. A cheap and easily prepared binding-protein is used and the procedure is suitable for clinical studies of cAMP concentrations in plasma.

In Vitro Effects of the Acylated StreptokinasePlasminogen Activator Complex BRL 33 575 Incubated with Normal Human Plasma

1984 ◽  
Vol 51 (03) ◽  
pp. 403-405 ◽  
Author(s):  
B Lämmle ◽  
G Noll ◽  
T H Tran ◽  
A Lohri ◽  
F Duckert
Keyword(s):  
Human Plasma ◽  
Clinical Studies ◽  
Systemic Effects ◽  
In Vitro Experiments ◽  
Normal Human Plasma ◽  
Normal Human ◽  
Repeated Doses ◽  
In Vitro Effects ◽  
Activator Complex

SummaryThrombolysis with acylated streptokinase-plasminogen complexes is aimed to achieve fibrinolysis without systemic fibrinogenolysis. The p-aminobenzoyl-streptokinase-(Lys)-plasminogen-complex (BRL 33 575) should be particularly useful due to its slow deacylation rate. Unexpectedly, repeated doses of 10 mg of BRL 33 575 (corresponding to 310'000 streptokinase equivalent units) induced systemic effects in patients though less than streptokinase alone. In vitro incubation of normal human plasma with BRL 33 575 at concentrations used in patients resulted in nearly complete consumption of α2-antiplasmin and plasminogen and significant fibrinogenolysis within 3 hr. This demonstrates that - despite of slow deacylation of BRL 33 575 - the small amounts of activator generated are highly efficacious in activating plasma plasminogen under conditions in which no physiological clearance of the free activator takes place. Simulating the calculated activator release from BRL 33 575 by infusing equivalent amounts of streptokinase into plasma resulted in less pronounced effects. This is probably explained by anti-streptokinase antibodies which will neutralize the initially infused streptokinase but will be bound by BRL 33 575.Our in vitro experiments indicate that further clinical studies should be done with lower doses of BRL 33 575 or prolonged dosage intervals.

Determination of unesterified fatty acids in normal human plasma

1958 ◽  
Vol 3 (5) ◽  
pp. 443-449 ◽  
Author(s):  
A. Svanborg ◽  
L. Svennerholm ◽  
J. Von Dorrien ◽  
M.R. Soomägi
Keyword(s):  
Fatty Acids ◽  
Human Plasma ◽  
Normal Human Plasma ◽  
Normal Human

The determination of vitamin C in normal human plasma and erythrocytes

1956 ◽  
Vol 1 (2) ◽  
pp. 167-177 ◽  
Author(s):  
Betty Iggo ◽  
J.A. Owen ◽  
C.P. Stewart
Keyword(s):  
Vitamin C ◽  
Human Plasma ◽  
Normal Human Plasma ◽  
Normal Human

scholarly journals Physicochemical properties of low-density lipoproteins of normal human plasma. Evidence for the occurrence of lipoprotein B in associated and free forms

1974 ◽  
Vol 137 (2) ◽  
pp. 155-167 ◽  
Author(s):  
Diana M. Lee ◽  
P. Alaupovic
Keyword(s):  
Human Plasma ◽  
Low Density ◽  
Separate Entity ◽  
Normal Human Plasma ◽  
Hydrodynamic Properties ◽  
Lipoprotein Subfractions ◽  
Normal Human ◽  
Preparative Ultracentrifugation ◽  
Association Complex

1. Low-density (d 1.006–1.063g/ml) lipoproteins from normal human plasma were separated by differential preparative ultracentrifugation into six subfractions. Each low-density (LD) lipoprotein subfraction contained lipoprotein B as the major and lipoproteins A and C as the minor lipoprotein families. 2. Three lipoprotein B subfractions (LP-B), LP-B-III (d 1.019–1.030g/ml), LP-B-IV (d 1.030–1.040g/ml) and LP-B-V (d 1.040–1.053g/ml) were prepared from the corresponding LD lipoprotein subfractions by immunoprecipitating small amounts of lipoproteins A and C. 3. Determination of hydrodynamic properties indicated that LD lipoproteins consisted of three molecular segments characterized by a stepwise change in the molecular weight: LDL-I and LDL-II subfractions (d 1.006–1.019g/ml) with an average mol.wt. of 4.75X106, LDL-III (d 1.019–1.030g/ml) with a mol.wt. of 3.99X106, and LDL-IV, LDL-V and LDL-VI (d 1.030–1.063g/ml) with a mol.wt. of 2.85X106. 4. All three lipoprotein B subfractions had an average mol.wt. of 3.16X106. 5. The LDL-I and LDL-II subfractions consisted of lipoprotein B and lipoprotein C families which were present in the form of an association complex. This was isolated from serum by immunoprecipitation with antibodies to lipoprotein B. The complex had a mol.wt. of 4.35X106. 6. The results indicate a fundamental difference between the LD lipoprotein subfractions with d 1.006–1.019g/ml and those subfractions with d 1.030–1.063g/ml. In the former, lipoprotein B occurs as a part of an association complex, whereas in the latter it occurs as a separate entity.

Performances of an Artificial Reagent for the One-stage Factor IX Assay

1975 ◽  
Vol 33 (03) ◽  
pp. 547-552 ◽  
Author(s):  
L Meunier ◽  
J. P Allain ◽  
D Frommel
Keyword(s):  
Human Plasma ◽  
Factor Ix ◽  
Severe Haemophilia ◽  
Normal Human Plasma ◽  
Haemophilia B ◽  
One Stage ◽  
Normal Human ◽  
The One

SummaryA mixture of adsorbed normal human plasma and chicken plasma was prepared as reagent for factor IX measurement using a one-stage method. The substrate was found to be specific for factor IX. Its performances tested on samples displaying factor IX activity ranging from <l%–2,500% compared favorably with those obtained when using the plasma of severe haemophilia B patients as substrate.

Sign in / Sign up

Export Citation Format

Share Document