Separation of water soluble proteins in psoriatic scales with different polyacrylamide gel concentrations and molecular weight estimations of the separated bands by disc-electrophoresis

1974 ◽  
Vol 250 (3) ◽  
pp. 245-252 ◽  
Author(s):  
Birgit Hook ◽  
Anita Neufahrt ◽  
Gottfried Leonhardi
2015 ◽  
Vol 43 (1) ◽  
pp. 27-37
Author(s):  
A. Pawłowski

A method for the preparation of a trypsin inhibitor from starchy endosperm of rye seeds is described. Isolation and purification comprised the following steps: salting out of the water-soluble proteins at pH 4.5 with ammonium sulphate (0.4 saturation), followed by chromatography on CM-Cellulose, Sephadex G-100 and SE Sephadex C-25. The finally purified preparation of inhibitor was found to be homogeneous by both chromatographic and electrophoretic analyses. The preparation inhibited trypsin and chymotrypsin but was inactive against papain, kallikrein and pepsin. The molecular weight of the inhibitor was calculated to foe about 10 000.


1987 ◽  
Vol 8 (3) ◽  
pp. 203-211
Author(s):  
Michael Veith

AbstractPolyacrylamide disc electrophoresis was carried out on water soluble proteins of eggs and embryos of Triturus alpestris, T. boscai, T. cristatus, T. helveticus, T. marmoratus and T. vulgaris. "Major bands" and "minor bands" were defined and species specific phenotyps are described. The patterns of major bands proved to be rather constant during embryonic development up to approximately stage 30 (stretched tailbud stage). The method as used in this study is considered to be practical and relevant for diagnostic studies on Triturus species.


1975 ◽  
Vol 252 (2) ◽  
pp. 85-90 ◽  
Author(s):  
Franz Jochen F�rster ◽  
Salim Balikcioglu ◽  
Gottfried Leonhardi

1969 ◽  
Vol 47 (12) ◽  
pp. 1823-1831 ◽  
Author(s):  
A. N. Glynn ◽  
J. Reid

Buffer-soluble proteins extracted from 33 isolates of various Fusarium oxysporum formae speciales and 13 other Fusarium species were separated on polyacrylamide gel disc electrophoresis. The resulting patterns were compared and their use as a taxonomic criterion assessed. The results obtained do not support the current concept that this method is useful as a taxonomic tool.


1968 ◽  
Vol 127 (2) ◽  
pp. 341-357 ◽  
Author(s):  
Marilyn Sue Kozak ◽  
Helmut H. Hahn ◽  
William J. Lennarz ◽  
W. Barry Wood

Small quantities of highly purified granulocytic pyrogen have been separated from contaminating proteins by disc electrophoresis in polyacrylamide gel. The biologically active material thus isolated was shown to be electrophoretically homogeneous at pH 9 and pH 3.8. Earlier work on the chemical properties of the pyrogen molecule has been extended to include: (a) estimation of its molecular weight by gel filtration; (b) demonstration of free sulfhydryl groups essential for its biological activity; and (c) evidence that it is not inactivated by exhaustive extraction with ethanolether or n-heptane.


1976 ◽  
Vol 35 (02) ◽  
pp. 295-304 ◽  
Author(s):  
B Østerud ◽  
M Miller-Andersson ◽  
U Abildgaard ◽  
H Prydz

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.


1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.


2013 ◽  
Vol 13 (3) ◽  
Author(s):  
Netty Widyastuti ◽  
Teguh Baruji ◽  
Henky Isnawan ◽  
Priyo Wahyudi ◽  
Donowati Donowati

Beta glucan is a polysaccharide compound, generally not soluble inwater and resistant to acid. Beta glucan is used as an immunomodulator (enhancing the immune system) in mammals is usually a beta-glucan soluble in water, easily absorbed and has a low molecular weight. Several example of beta-glucan such as cellulose (β-1 ,4-glucan), lentinan (β-1 0.6-glucan) and (β-1 ,3-glucan), pleuran (β-1, 6 and β-1 ,3-glucan) are isolated from species of fungi Basidiomycota include mushrooms (Pleurotus ostreatus) and shiitake (Lentinus edodes).The purpose of thisresearch activity is to obtain beta-glucan compound that can be dissolved in water and in alkali derived from fungi Basidiomycota, i.e, Oyster mushrooms (Pleurotus ostreatus) and shiitake (Lentinus edodes). The result of beta-glucan compared to characterize the resulting beta glucan that is molecular structure . The difference of beta glucan extraction is based on the differences in solubility of beta-glucan. Beta glucan could be water soluble and insoluble water.


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