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KMID : 0376219790160010021
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Chonnam Medical Journal
1979 Volume.16 No. 1 p.21 ~ p.25
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Changes in Electrophoretic Patterns of Human Serum Proteins after Cross-Electrophoresis with Trypsin
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Abstract
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Human serum proteins were cross-electrophoresed against bovine pancreatic trypsin at pH 8.6 on cellulose acetate membrane, and changes in the electrophoretic profile was studied.
The alph1-globulin fraction which appeared faint in the absence of trypsin became prominent after crossing with trypsin. The albumin and other globulin fractions were decreased after crossing with trypsin. Evidence was presented to indicate that the augmented visualization of alpha,-globulin fraction by trypsin crossing is not due to the formation of alpha1 -antitrypsin-trypsin complex, but rather derived from the partially digested albumin by trypsin. This also afforded an explanation for the decrease in the albumin fraction after trypsin-crossing.
Cross-electrophoresis of human serum against 131I-labeled trypsin clearly indicated retardation in the mobility of alpha1-antitrypsin-trypsin complex. This finding was also revealed by an oblique cross-electrophoresis of human serum against trypsin.
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