Structure of Helix pomatia Oxy-beta-hemocyanin and Deoxy-beta-hemocyanin Tubular Polymers
1979; Wiley; Volume: 100; Issue: 1 Linguagem: Inglês
10.1111/j.1432-1033.1979.tb02033.x
ISSN1432-1033
AutoresJan F. L. van Breemen, Jan H. Ploegman, E.F.J. Van Bruggen,
Tópico(s)Blood properties and coagulation
ResumoMild trypsinolysis of Helix pomatiaβ-hemocyanin leads to the formation of tubular polymers after removal of the collar part [van Breemen, J. F. L., Wichertjes, T., Muller, M. F. J., van Driel, R., and van Bruggen, E. F. J. (1975) Eur. J. Biochem. 60, 129–1351]. Three-dimensional image reconstruction from electron micrographs of negatively stained tubular polymers showed: (a) alternating deep and shallow grooves in between the 10 helical chains, (b) the presence and position of two domains within each morphological wall-unit of the Mellema and Klug model [Mellema, J. E. and Klug, A. (1972) Nature (Lond.) 239, 146–150]. Optical diffraction of oxy and deoxygenated tubular polymers indicate a significant decrease in diameter with a concomitant increase in length upon deoxygenation.
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