The Study of Type I Collagen by Immunoblotting in Samples of Bone-Plastic Biomaterials

The type I collagen was studied in samples of two types osteoplastic materials produced the Biotech Research Institute Samara State Medical University using immunoblotting. demineralized used work were compact bone powder and crushed material human cancellous tissue. Collagen its polypeptides separated a 5% polyacrylamide gel with 3.6 M urea according to method Hayashi Nagai (1979). advantage is separation under these conditions III collagen, as well α1(I) α2(I) chains collagen. Immunoblotting carried out by diffusion Towbin et al. (1979) nitrocellulose membranes (Santa Cruz, USA). Primary goat polyclonal antibodies denatured 1:500 dilution (Millipore) used. Peroxidase-conjugated secondary (mouse vs. goat), 1:80000 (Sigma) also. It has been established that bulk protein localized between α1- α2-fractions In tissue, molecular reduction noted. Protein macromolecules gradually decreasing weight low migrating wide front up indicator line are detected. Due specificity osteoblast integrins regenerating polypeptides, molecules retained implants, can act inducers synthetic processes occurring nuclei. fragmentation products implant signaling trigger cascades enzymatic reactions intracellular pathways.