Differences in ultrastructural organization of amyloid as revealed by sensitivity or resistance to induced proteolysis

Author:

Romh�nyi Georg

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology,General Medicine,Pathology and Forensic Medicine

Reference55 articles.

1. Arvy, L., Sors, C.: Etude histochimique de la substance amyloide. Acta histochem. (Jena) 6, 77?92 (1958).

2. Benditt, E. P., Eriksen, N.: Amyloid. II. Starch gel electrophoretic analysis of some proteins extracted from amyloid. Arch. Path. 78, 325?330 (1964).

3. Benditt, E. P., Eriksen, N.: Chemical classes of amyloid substance. Amer. J. Path. 65, 231?252 (1971).

4. Bladen, H. A., Nylen, M. U., Glenner, G. G.: The ultrastructure of human amyloid as revealed by the negative staining technique. J. Ultrastruct. Res. 14, 449?459 (1966).

5. Braunstein, H., Buerger, L.: A study of the histochemical and staining characteristics of amyloid. Amer. J. Path. 35, 791?800 (1959).

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