Fiber Formation in Trypsinogen Solutions: An Electron Optical Study.
- 1 October 1951
- journal article
- research article
- Published by Frontiers Media SA in Experimental Biology and Medicine
- Vol. 78 (1) , 241-244
- https://doi.org/10.3181/00379727-78-19034
Abstract
The coiled threads and filaments described by Gross as essential components of elastin, liberated from the tissue by tryptic digestion, and later described by Franchi and De Robertis as products of tryptically digested bacterial flagellae were demonstrated to be present in Armour''s crystalline trypsin, but not in the more highly purified product "Tryptar," and could be produced by incubation from clear, sterile solns. of crystalline trypsinogen. This process probably represented a fibrous transformation of trypsinogen, a component or contaminant thereof.Keywords
This publication has 3 references indexed in Scilit:
- THE STRUCTURE OF ELASTIC TISSUE AS STUDIED WITH THE ELECTRON MICROSCOPEThe Journal of Experimental Medicine, 1949
- Tropomyosin: a new asymmetric protein component of the muscle fibrilBiochemical Journal, 1948
- STUDIES OF ACTIN AND MYOSIN1947