Hämoglobine, XXXVI. Die Primärstruktur eines dimeren Insektenhämoglobins (Erythrocruorin) (CTT IX)(Chironomus thummi thummi). Versuche zur Quartärstruktur der dimeren CTT-Hämoglobine

Publisher Website
Google Scholar
Abstract
The primary structure of a dimeric insect HB (erythrocurorin), component CTT IX (C. T. thummi) was established by automatic sequence analysis. The alignment of the peptides was facilitated by producing only a few large fragments. The primary structure of CTT IX is compared with the human B-chains and with CTT III. The reason for the dimeric CTT Hb dimerisation can be observed, but no tetramerization is discussed. Experiments were done to locate the binding areas between the subunits in the dimeric molecule. Even after blocking of the a-NH2-group by cyanate, the stability of the dimeric molecule is not altered. The binding regions of the CTT Hb must differ from those of the tetrameric Hb of vertebrates. A quarternary structure different from that of the Hb of mammal is found. This structure explains the possibility of dimerization, but excludes tetramerization.

This publication has 25 references indexed in Scilit: