Fractionation of Plasminogen by Starch Gel Electrophoresis
1964 ◽
Vol 12
(01)
◽
pp. 126-136
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Keyword(s):
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.
1961 ◽
Vol 236
(7)
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pp. 1986-1990
1963 ◽
Vol 41
(1)
◽
pp. 369-387
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1967 ◽
Vol 120
(2)
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pp. 255-267
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Keyword(s):
1999 ◽
Vol 27
(5)
◽
pp. 499-505
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1990 ◽
Vol 46
(8)
◽
pp. 863-867
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1963 ◽
Vol 41
(12)
◽
pp. 2507-2516
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Keyword(s):
1968 ◽
Vol 25
(12)
◽
pp. 2651-2663
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Keyword(s):