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Last Updated: 3 years ago

Possible Interaction: Trypsin and Rabbit Allergenic Extract

Research Papers that Mention the Interaction

Treatment of erythrocytes with Clostridium perfringens sialidase or trypsin increased four-fold the activity toward rabbit erythrocytes and positive agglutination for human A and B erythrocytes, suggesting the presence of FVIII/VWF-cryptic receptors in these erythrocytes.
The Tohoku journal of experimental medicine  •  2009  |  View Paper
Loss of the hemagglutination activity was observed when rabbit erythrocytes were treated with trypsin or neuraminidase.
Current Microbiology  •  2004  |  View Paper
Reduction of haemagglutination activity by pretreatment of rabbit erythrocytes with trypsin or neuraminidase solutions further supports this view.
Annales de l'Institut Pasteur. Microbiology  •  1987  |  View Paper
Trypsin digestion considerably reduced the ability of pig and bovine transferrins to donate iron to rabbit reticulocytes, slightly reduced the iron-donating ability of rabbit transferrin, and had almost no effect on that of human or horse transferrins.
Biochimica et biophysica acta  •  1980  |  View Paper
Activation of rabbit Hageman factor with trypsin resulted in cleavage of the molecule into three fragments, each of 30,000 mol wt as noted previously.
The Journal of experimental medicine  •  1973  |  View Paper
Calf, horse and rabbit serum inhibited the growth stimulating effect of trypsin but chicken, dog and monkey serum were permissive.
Journal of cellular physiology  •  1977  |  View Paper
This trypsin labile activity causes a dose-dependent relaxation of rabbit aorta and chicken rectum assay strips.
Biochemical and biophysical research communications  •  1984  |  View Paper
Trypsin stimulated adenylyl cyclase activity in rabbit corpus luteum membranes.
Biology of reproduction  •  1979  |  View Paper
The zona pellucida of the mouse (4-6), rat and rabbit was shown to be more resistant to digestion by trypsin after fertilization than before (2).
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine  •  1971  |  View Paper
Abstract Glyceraldehyde-3-phosphate dehydrogenases from rabbit muscle, yeast and Ehrlich ascites tumor cells were inactivated by trypsin at 25 ° to the extent of 4, 25, and 46%, respectively.
Archives of biochemistry and biophysics  •  1971  |  View Paper