Disc-electrophoresis of modified human globin in stepwise gradient of concentration of polyacrylamide gel

1969 ◽  
Vol 34 (8) ◽  
pp. 2478-2481
Author(s):  
S. Ulrych
Keyword(s):  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Stepwise Gradient

The Effect of Antithrombin III on the Activity of the Coagulation Factors VII, IX and X

1976 ◽  
Vol 35 (02) ◽  
pp. 295-304 ◽  
Author(s):  
B Østerud ◽  
M Miller-Andersson ◽  
U Abildgaard ◽  
H Prydz
Keyword(s):  
Antithrombin Iii ◽  
Factor Xa ◽  
Coagulation Factors ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Factor Vii ◽  
Native Form ◽  
Factor Ixa ◽  
Plasma Factor

SummaryAntithrombin III, purified to homogeneity according to Polyacrylamide gel disc electrophoresis and immunoelectrophoresis, inhibited the activity of purified factor IXa and Xa, whereas factor VII was not inhibited either in the active or in the native form.Antithrombin III is the single most important inhibitor of factor Xa in plasma. Factor Xa does not, however, reduce the activity of antithrombin III against thrombin.

Structure Abnormality Of Fibrinogen Metz And Its Relationship To The Clotting Defect

1981 ◽  
Author(s):  
A Henschen ◽  
C Southan ◽  
J Soria ◽  
C Soria ◽  
M Samama
Keyword(s):  
Young Woman ◽  
Sodium Citrate ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Fibrinopeptide A ◽  
Clotting Time ◽  
Terminal Part ◽  
Fibrin Formation ◽  
No Release ◽  
Α Chain

Fibrinogen Metz was discovered in a young woman and was associated with a mild bleeding disorder and repeated abortions. Her parents are cousins and both have an abnormal fibrin formation but less intense than in the propositus.Fibrinogen Metz is therefore an homozygous case characterized by an unclottability of citrated sample, even in the presence of calcium and large quantities of thrombin. In addition, the clotting time is prolonged when the blood is collected in the absence of sodium citrate and the clot is extremely weak.By immunoenzymological assay, no release of fibrinopeptide A was noted after thrombin addition to purified fibrinogen. Furthermore, by disc electrophoresis in polyacrylamide gel in absence of SDS, an abnormal migration of the A α chain was observed.These results led us to analyze the sequence of the N terminal part of the A α chain by the Edman procedure. Arginine in position 16 was replaced by cysteine in fibrinogen Metz. This mutation localized on the site cleaved by thrombin explains the absence of fibrinopeptide A release, and the abnormal clottability of fibrinogen Metz.

Quantitation of Beta Lipoprotein (LDL) Cholesterol by Densitometric Evaluation of Disc Electropherograms

1972 ◽  
Vol 18 (3) ◽  
pp. 217-221 ◽  
Author(s):  
Robert F Moran ◽  
William P Castelli ◽  
Marianne V Moran
Keyword(s):  
Ldl Cholesterol ◽  
Electrophoretic Pattern ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Type Ii ◽  
Chemical Concentration ◽  
Type Iv ◽  
Chemical Technique ◽  
Peak Areas

Abstract This paper describes a rapid, facile, and accurate new procedure for determination of marginal Type IV or Type II hyperlipoproteinemias, in which discontinuous (disc) electrophoresis on polyacrylamide gel is used to quantitate LDL (beta) cholesterol without ultracentrifugation. Fasting sera, previously assayed by ultracentrifugation and chemical technique, were prestained with Sudan Black, and the lipoproteins were separated by disc electrophoresis. The beta-lipoprotein fraction of each electrophoretic pattern was quantitated by densitometry. The values for the integrated densitometric peak areas for the beta fraction and the chemically assayed cholesterol of the ultracentrifuged LDL fraction correlated well (r = .90). Results were determined from a curve relating chemical concentration of the integrated peak values by densitometry to the known LDL cholesterol of a series of standards.

scholarly journals Purification and properties of β-mannanases I and II from the germinated seeds of Trifolium repens. Mode of galactomannan degradation in vitro

1978 ◽  
Vol 175 (3) ◽  
pp. 1079-1087 ◽  
Author(s):  
H Villarroya ◽  
J Williams ◽  
P Dey ◽  
S Villarroya ◽  
F Petek
Keyword(s):  
Trifolium Repens ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Ph Optimum ◽  
Electrophoretic Method ◽  
Germinated Seeds

Two beta-mannanases (beta-mannosidases, EC 3.2.1.25) purified from the germinated seeds of Trifolium repens by a procedure that included chromatography on hydroxyapatite, gel filtration on acrylamide/agarose (Ultragel 5/4) and preparative polyacrylamide-gel-electrophoresis. The final purification step completely resolved two beta-mannanases with distinct specificities, which were termed beta-mannanase I and beta-mannanase II. beta-Mannanase I was purified 1400-fold and beta-mannanase II 1000-fold. The purified enzymes showed a single protein band when examined by polyacrylamide-gel disc electrophoresis. beta-Mannanase I, apparent mol.wt. 43 000, accounted for 49% of the total activity recovered from the final step of purification. beta-Mannanase II, apparent mol.wt. 38 000, accounted for the remaining 51% of activity. Molecular-weight determinations were by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and by the electrophoretic method of Hendrick & Smith [(1968) Arch. Biochem. Biophys. 126, 155-164]. The substrate specificities of both enzymes were examined with the galactomannans of T. repens and of Medicago sativa, as well as with manno-oligosaccharides. The pH optimum was between pH 5.1 and 5.6 for both enzymes.

scholarly journals Isolation and separation of α and β-tubulin from chick-embryo brain, muscle and skin

1978 ◽  
Vol 169 (3) ◽  
pp. 717-719
Author(s):  
A R A el-Hamalawi
Keyword(s):  
Chick Embryo ◽  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
New Method ◽  
Embryo Brain ◽  
Β Tubulin

Two kinds of tubulin, alpha and beta, have been described in microtubules from many different systems. In the present study a new method is described for isolating and separating these two kinds of tubulin from chick-embryo brain, muscle and skin. The isolated tubulins were characterized by polyacrylamide-gel disc electrophoresis in the presence of urea and sodium dodecyl sulphate.

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