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PMID: 1237295 Published · ppublish English Journal Article

The reaction of penicillin with proteins.

The Biochemical journal ·Vol. 149 ·No. 2 ·1975-08-00 ·Pages 357-64

Corran PH, Waley SG

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.

MeSH Terms
Amino Acids/analysis Animals Binding Sites Chickens Drug Hypersensitivity Egg White Humans Insulin Kinetics Muramidase Penicillin G Peptide Fragments/analysis Protein Binding Swine
Chemicals
Amino Acids Insulin Peptide Fragments Muramidase Penicillin G
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Corran P H
Waley S G
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30 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1975-08-00
Pages
357-64
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1165629
Subset
IM
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