Abstract
IN the assay of secretin by Love's method1 in which pancreatic secretion from the fasted rat is collected in calibrated capillary tubes, it was observed that a slight precipitate very occasionally formed in the tube at room temperature. When the secretion was kept at +2° C. a heavy white deposit almost invariably formed within two days or so which consisted of very fine birefringent needles, often in balls, fans, or sheaves (Fig. 1). The difference in ultra-violet absorption of the secretion before and after formation of the deposit (Fig. 2) suggested that the latter might be a protein. Further experiments showed it to be amylase, and it became of interest to compare its properties with those of crystalline pancreatic α-amylase from human2 and pig3.
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References
Love, J. W., Quart. J. Physiol., 42, 279 (1957).
Fischer, E. H., Duckert, F., and Bernfeld, P., Helv. chim. Acta, 33, 1060 (1950).
Meyer, K. H., Fischer, E. H., and Bernfeld, P., Arch. Biochem., 14, 149 (1947).
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Sumner, J. B., and Howell, S. F., J. Biol. Chem., 108, 51 (1935).
Bernfeld, P., “Adv. Enzymol.”, 12, 379 (1951).
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HEATLEY, N. Spontaneous Crystallization of Amylase from Pancreatic Juice of the Rat. Nature 181, 1069–1070 (1958). https://doi.org/10.1038/1811069a0
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DOI: https://doi.org/10.1038/1811069a0
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