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. 1975 Aug;149(2):357–364. doi: 10.1042/bj1490357

The reaction of penicillin with proteins.

P H Corran, S G Waley
PMCID: PMC1165629  PMID: 1237295

Abstract

The mode of reaction of benzylpenicillin with two proteins was studied, with particular reference to the allergenicity of penicillin. These reactions, with pig insulin, and with hen's-egg-white lysozyme, were carried out in neutral solution at 37 degrees C. High concentrations of penicillin are needed to label the proteins, owing to concurrent hydrolysis of penicillin. Evidence has been obtained that the penicillin-reactive sites on the insulin molecule are the alpha-amino group at the N-terminus of the A chain and the epsilon-amino group of the lysine residue; whereas a site of reaction with lysozyme appears to be the epsilon-amino group of lysine-116.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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