Big Book by Pam Bono

By Pam Bono

Книга по пэчворку и квилтингу.

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1981). In "Ab­ stracts, Seventh American Peptide Symposium", p. 93. S. (1980). W. ), p. 29. Science Press, Beijing. S. (1981). Sei. Sin. 24, 264. STUDIES ON THE THREE-DIMENSIONAL STRUCTURE OF INSULIN AND ITS ANALOGS1 Liang Dong-cai2 Institute of Biophysics Chinese Academy of Sciences Beijing Since Banting and Best discovered insulin, as a result of their work on diabetes, it has been the object of intensive research during the past sixty years. Insulin is one of the smallest protein molecules and has a very complicated biolog­ ical activity.

Hoppe-Seyler's 350, 741. Hor. Res. 27, Z. Physiol. 1. Chem. -P. et al. (1980). Scientia Sinica 23, 1309. F. et al. (1975). Acta Crust. S, 21. H. (1977). Diabetologia 13, 257. T. et al. -J. et al. -Y. et al. (1965). (1980). (1980). Scientia Sinica 14, Scientia Sinica 23, 1443. Progress 1710. in Biochemistry and Biophysics 4, 43 (in Chinese). -Z. et al. (1980). Scientia Sinica 23, 1593. Scientia Peking Insulin Structure Research Group (1972). Sinica 15, 3. Peking Insulin Structure Research Group (1974).

The approach involved covalently linking thrombin to small polystyrene beads which could not enter cells. By using carboxylate-modified beads and a water-soluble carbodiimide reagent, it was possible to link the thrombin to the beads by a peptide bond. Of several linkages tried, this one was the most stable. The thrombin that was linked to the beads in these experiments was labeled to a very high specific radioactivity with Ί 25j s o that its release from the beads could be sensitively monitored.

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