Pork insulin recombined from cleaved A- and B-chains of pancreatic insulin was shown to be identical with the pancreatic hormone both in erythrocyte receptor assays and in immunoassays employing four different antisera, including two species-specific human anti-insulin sera. Pancreatic human insulin and that prepared from recombined bacterially synthesized A- and B-chains were also indistinguishable in the same systems. This study demonstrates that the prohormone stage of either human or porcine insulin is not required to preserve potency of membrane binding or immunochemical reactivity, even employing an antiserum with marked species specificity.

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