Letter | Published:

X-Ray Photographs of Crystalline Pepsin

Naturevolume 133pages794795 (1934) | Download Citation



FOUR weeks ago, Dr. G. Millikan brought us some crystals of pepsin prepared by Dr. Philpot in the laboratory of Prof. The Svedberg, Uppsala. They are in the form of perfect hexagonal bipyramids up to 2 mm. in length, of axial ratio c/a = 2.3 ± 0.1. When examined in their mother liquor, they appear moderately birefringent and positively uniaxial, showing a good interference figure. On exposure to air, however, the birefringence rapidly diminishes. X-ray photographs taken of the crystals in the usual way showed nothing but a vague blackening. This indicates complete alteration of the crystal and explains why previous workers have obtained negative results with proteins, so far as crystalline pattern is concerned1. W. T. Astbury has, however, shown that the altered pepsin is a protein of the chain type like myosin or keratin giving an amorphous or fibre pattern.

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  1. 1

    G. L. Clark and K. E. Korrigan (Phys. Rev., (ii), 40, 639; 1932) describe long spacings found from crystalline insulin, but no details have been published.

  2. 2

    J. H. Northrop, J. Gen. Physiol., 13, 739 ; 1930.

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  1. Department of Mineralogy and Petrology, Cambridge

    • J. D. BERNAL
    •  & D. CROWFOOT


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