Abstract
So-called Sericin-cocoons which do not contain any amount of fibroin have been treated with cupriethylenediamine solution to transfer the sericin molecules quantitatively from insoluble form to water soluble globular one. The sericin aqueous solutions, thus obtained, have been analyzed by means of electrophoresis, ultracentrifuge or diffusion measurements comparing with other described sericin preparations and also with soluble proteins extracted from silk-glands of mature Sericin-cocoon-forming silkworms or normal ones.
The results show that 1) all the previous sericin fractions such as MOSHER'S A and B or HAYASHI and ODA'S α and β must be the heat denaturation and/or degradation products, and native sericin can not consist of other than only one component with the isoelectric point of pH 4. 2, 2) there may be a unique dissociation-association system in sericin solution and 3) there might be such a kind of interaction between fibroin and sericin as to change the latter only to gel form, which might suggest the mechanism of naturally occurring selective coagulation of silk proteins.
