Human Prothrombin

1970 ◽  
Vol 24 (03/04) ◽  
pp. 311-324 ◽  
Author(s):  
Th. R Derleth ◽  
J. A Penner
Keyword(s):  
Cellulose Acetate ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
High Specific Activity ◽  
Factor Ix ◽  
Factor Vii ◽  
Starch Gel Electrophoresis ◽  
Multiple Protein ◽  
Starch Gel

SummaryA method is presented for the chromatographic separation of human prothrombin from variable volumes of plasma. The procedure is simple, consisting of chromatography on ECTEOLA which provides a potent product containing factor IX and X activity sufficient for therapeutic use. Additional chromatography on DEAE or Sephadex G200 will produce a prothrombin of high specific activity which appears homogeneous by ultracentrifugation and electrophoresis on cellulose acetate, although multiple protein fractions can be identified on starch gel electrophoresis.Human prothrombin prepared by this method migrates as an alpha 2-globulin and does not appear to be altered electrophoretically or antigenically from its original state in the plasma. The characteristics of human prothrombin obtained from patients with deficiencies of factor VII or IX do not differ from normal.

scholarly journals Clonal variation within a mucosal isolate derived from a patient with Leishmania (Viannia) braziliensis infection

1991 ◽  
Vol 33 (5) ◽  
pp. 343-350 ◽  
Author(s):  
César Augusto Cuba-Cuba ◽  
David Evans ◽  
Ana de Cassia Rosa ◽  
Philip Davis Marsden
Keyword(s):  
Monoclonal Antibodies ◽  
Cellulose Acetate ◽  
Phenotypic Variation ◽  
Gel Electrophoresis ◽  
Clonal Variation ◽  
Starch Gel Electrophoresis ◽  
Mucosal Leishmaniasis ◽  
Starch Gel

Three isolates over 5 years from a patient with persistent relapsing mucosal leishmaniasis due to Leishmania (Viannia) braziliensis and 7 clones from one of these isolates were studied by zymodemes and scrodemes analysis. Results showed evidences of clonal phenotypic variation. Eight isoenzymes markers demonstrated clear differences on Cellulose Acetate (CA) and thin starch gel electrophoresis. Also a panel of specific monoclonal antibodies showed such differences. Our observations provide additional evidence that Leishmania (Viannia) braziliensis is composed by subpopulations of parasites with peculiar biochemical and antigenic characteristics.

scholarly journals An Improved Chromatographic Separation of Wheat Gluten Proteins

1965 ◽  
Vol 18 (1) ◽  
pp. 193 ◽  
Author(s):  
CW Wrigley
Keyword(s):  
Column Chromatography ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Carboxymethyl Cellulose ◽  
Wheat Gluten ◽  
Starch Gel Electrophoresis ◽  
Gluten Proteins ◽  
Electrophoretic Patterns ◽  
Starch Gel

Gel electrophoresis is at present the best procedure for the analytical fractiona-tion of wheat gluten proteins. Procedures more suitable for preparative studies, such as gel ffitration and column chromatography, have provided only partial fractionation on the basis of gel electrophoresis (Graham 1963; Lee et al. 1963; Wright, Brown, and Bell 1964). Gel electrophoretic patterns of fractions resulting from the carboxymethyl cellulose (CMC) fractionation of Simmonds and Winzor (1961) have been published by Graham (1963) and by Lee et al. (1963). These results showed that each fraction was heterogeneous, with considerable overlapping of electrophoretic bands from neighbouring fractions, and that fractions eluted late in the chromatogram were contaminated because of tailing of earlier fractions. The modification of the Simmonds and Winzor procedure described below results in an improved fractionation of gluten proteins as judged by starch-gel electrophoresis.

Studies on the relation between plasma antithrombin and heparin-cofactor

1968 ◽  
Vol 46 (3) ◽  
pp. 347-350 ◽  
Author(s):  
F. C. Monkhouse ◽  
Susan Milojevic
Keyword(s):  
Gel Electrophoresis ◽  
Specific Activity ◽  
Deae Cellulose ◽  
Fold Increase ◽  
Significant Loss ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Starch Gel ◽  
Cofactor Activity ◽  
Cellulose Column

A method for the preparation of purified plasma antithrombin and heparin-cofactor is described. The method involves adsorption by aluminium hydroxide, separation on a DEAE-cellulose column by means of a graded salt concentration, and vertical curtain electrophoresis. A 100-fold increase in the specific activity of antithrombin and a 30-fold increase in the specific activity of heparin-cofactor have been achieved. In spite of the increased purification, no separation of the two activities was achieved. When a highly purified fraction was subjected to starch-gel electrophoresis for 16–18 h and then eluted from the gel, there was significant loss of heparin-cofactor activity but not of antithrombin activity. The electrophoretic patterns of the recovered proteins were not altered.

scholarly journals Further studies on the inheritance of lymph proteins in Drosophila melanogaster

1966 ◽  
Vol 7 (3) ◽  
pp. 287-294 ◽  
Author(s):  
E. J. Duke
Keyword(s):  
Drosophila Melanogaster ◽  
Cellulose Acetate ◽  
Gel Electrophoresis ◽  
Protein Fraction ◽  
Autosomal Gene ◽  
Single Pair ◽  
Starch Gel Electrophoresis ◽  
Dominant Allele ◽  
The Third ◽  
Starch Gel

The inheritance of three protein fractions of third instar larval lymph in Drosophila melanogaster as detected by starch gel electrophoresis is described. Each of the three is governed by a single autosomal gene. In two, the dominant allele determines presence, and the recessive absence of the respective fraction. The third protein fraction is governed by a single pair of co-dominant alleles.Comparison of the starch-gel pattern to that obtained on cellulose acetate and on polyacrylamide gel fails to show definite sub-fractionation of those protein bands of which the inheritance has been studied.

scholarly journals The Amino Acid Composition of Hemoglobin. V. The Preparation of Purified Hemoglobin Fractions by Chromatography on Cellulose Exchangers and Their Identification by Starch Gel Electrophoresis Using Tris-Borate-EDTA Buffer

Blood ◽  
1965 ◽  
Vol 25 (5) ◽  
pp. 646-661 ◽  
Author(s):  
AMOZ I. CHERNOFF ◽  
NELSON PETTIT ◽  
JO NORTHROP
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Tris Borate Edta

Abstract The chromatographic separation of hemoglobin on two cellulose exchangers, CMC and DEAE, is discussed. Problems related to the use of these technics are described. In addition, our experience with the use of Tris-Borate-EDTA buffer (Smithies) for hemoglobin electrophoresis in starch gel is presented.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

Sign in / Sign up

Export Citation Format

Share Document