The use of edestin in determining the proteolytic activity of pepsin
โ Scribed by Joseph F. Brewster
- Publisher
- Elsevier Science
- Year
- 1921
- Tongue
- English
- Weight
- 52 KB
- Volume
- 191
- Category
- Article
- ISSN
- 0016-0032
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Pepsin is of interest for many reasons, but attention is directed here to it as representing those enzymes that probably contain no prosthetic (nonamino acid) groups. Its proteolytic activity must, therefore, be attributed to the arrangement of its amino acids in the peptide chain and/or to the fold
The thyroglobulin molecule is of large size, with a molecular weight of about 700,000 (Heidelberger and Pedersen, '35), yet it passes rapidly into and out of the thyroid follicle of the mammal with no apparent intercellular spaces. Since cell membranes are not normally permeable 'Fellow in Anatomy.