[Synthesis of insulin fragments and study of their physicochemical and immunological properties].
A two-chain peptide was predicted as a receptor binding site of insulin on the basis of theoretical conformational analysis. This dimeric peptide, consisting of the C-terminal A18-A21 tetrapeptide of the insulin A-chain and the C-terminal B17-B30 tetradecapeptide of the insulin B-chain connected with a disulfide bridge, was synthesized along with the C-terminal nonadecapeptide. The analysis of the aggregation state of human insulin and the synthesized linear and dimeric peptides was performed by the small-angle X-ray scattering method. Specific antibodies were produced after rabbit immunization with the dimeric peptide-BSA conjugate. The immunochemical identity of the model dimeric peptide and the corresponding fragment of the insulin molecule were shown by immunoenzyme analysis.
Panin
L E
LE
Institute of Biochemistry, Siberian Division, Russian Academy of Medical Sciences, Novosibirsk, Russia.
Tuzikov
F V
FV
Poteriaeva
O N
ON
Maksiutov
A Z
AZ
Tuzikova
N A
NA
Sabirov
A N
AN
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D007114:Immunization; D007124:Immunoenzyme Techniques; D007150:Immunohistochemistry; D007328:Insulin / Q000138:chemical synthesis* / Q000276:immunology / Q000378:metabolism; D007330:Insulin Antibodies / Q000032:analysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000276:immunology / Q000378:metabolism; D011487:Protein Conformation; D011817:Rabbits; D011972:Receptor, Insulin / Q000276:immunology / Q000378:metabolism; D014961:X-Ray Diffraction
D007328:Insulin; D007330:Insulin Antibodies; D010446:Peptide Fragments; D011972:Receptor, Insulin
Sintez fragmentov insulina i izuchenie ikh fiziko-khimicheskikh i immunologicheskikh svoĭstv.