PROINSULIN: CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES
- 1 August 1970
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 66 (4), 1213-1219
- https://doi.org/10.1073/pnas.66.4.1213
Abstract
Bovine proinsulin has been crystallized under a variety of conditions at both neutral and acid pH. Microtechniques were employed with sample weights of about 200 mug and volumes of 5-20 mul. The crystalline preparations all differ from each other morphologically.X-ray photographs of one form, tetragonal bipyramids grown at pH 3 with added ammonium sulphate solution, established the space group P4(1)2(1)2 (or its enantiomorph P4(3)2(1)2). The cell dimensions are a = 50.8 +/- 0.2 A, c = 148.0 +/- 0.4 A. The asymmetric unit in this form is a dimer of proinsulin which is also the dominant species in solution at this pH.Keywords
This publication has 14 references indexed in Scilit:
- Interaction of zing with proinsulinBiochemical and Biophysical Research Communications, 1970
- Isolation of a proinsulin connecting peptide fragment (C-peptide) from bovine and human pancreasBiochemical and Biophysical Research Communications, 1969
- Isolation and Properties of Proinsulin, Intermediate Forms, and Other Minor Components from Crystalline Bovine InsulinDiabetes, 1968
- Prediction of alpha-helical regions in proteins of known sequence.Proceedings of the National Academy of Sciences, 1968
- Micro diffusion cells for the growth of single protein crystals by means of equilibrium dialysisArchives of Biochemistry and Biophysics, 1968
- Physical studies on proinsulin — Association behavior and conformation in solutionBiochemical and Biophysical Research Communications, 1968
- Amino acid composition of bovine ‘proinsulin’Biochemical and Biophysical Research Communications, 1967
- Insulin Biosynthesis: Evidence for a PrecursorScience, 1967
- THE BIOSYNTHESIS OF INSULIN AND A PROBABLE PRECURSOR OF INSULIN BY A HUMAN ISLET CELL ADENOMAProceedings of the National Academy of Sciences, 1967
- An Equilibrium Ultracentrifuge Study of the Self-Association of Bovine Insulin*Biochemistry, 1966