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Association of poly-(L-lysine) homologues in sodium carbonate solution
Authors:K Kakiuchi  A Tsuboi
Institution:(1) Present address: Institute for Protein Research, Osaka University, Suita, Japan
Abstract:The molecular weights of isopoly(L-Iysine), poly(L-ornithine), and poly(L-agr, gamma-diaminobutylic acid), the homologues of poly (L-lysine), were determined by the sedimentation equilibrium method in aqueous solutions of 1.0 M NaCl or 0.1 M Na2CO3. In every sample the molecular weights in the presence of carbonate ions was twice that in NaCl solution. In a previous paper we reported that poly(L-lysine) behaved as a dimer at concentrations higher than 0.4 g/dl in the presence of carbonate ions and as a monomer in dilute solution, and these two forms were related by a monomer-dimer equilibrium. The homologues did not have a monomer-dimer equilibrium relationship under the conditions of the measurements that we carried out. The CD spectrum of isopoly(L-lysine) in water showed a uniform increase with a decrease in the wave length in the presence of carbonate ions. However, in the alkaline region in NaOH solution, the spectrum changed and a small minimum at 212 nm was found. When additional carbonate ions were added a large minimum at 205 nm was observed. This result can be explained by a change in the conformation from a random coil to a regular structure. We could not compare isopoly(L-lysine) with other polypeptides, because it does not have peptide bonds. The CD spectra of poly(L-ornithine) and poly(L-agr, gamma-diaminobutylic acid) in NaOH or Na2CO3 solutions showed only slightly regular structures. It was also confirmed that the dimer-structures of the poly (L-lysine) homologues do not have regular structures.This paper was presented at the ldquoVI. Symposium on Analytical Ultracentrifugationrdquo, Marburg, FRG, February 16–17,1989.
Keywords:Poly(L-lysine)homologues  sedimentationequilibrium  circulardichroismmeasurement  sodiumcarbonate  dimer  conformationalanalysis  carbamatestructure
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