AI Article Synopsis
- Recombinant [B18Ile] human insulin was produced from a specialized mutant PIP through a process called transpeptidation.
- This insulin variant can form crystals and exhibits 82% of the receptor binding capability compared to porcine insulin, maintaining similar biological effects in live organisms.
- The study suggests that the B18Val residue does not play a significant role in how insulin functions biologically.
Article Abstract
Recombinant [B18Ile] human insulin was obtained from a mutant [B18Ile] PIP purified by transpeptidation. [B18Ile] human insulin can be crystallized and has 82% of receptor binding activity as that of porcine insulin and retains almost the same level of in vivo biological activity comparing with porcine insulin. It is proposed that the B18Val residue may not be involved in the expression of insulin activity.
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