Studies on the direct neutral penicilloylation of functional groups occurring on proteins

作者: C.H. Schneider , A.L. De Weck

DOI: 10.1016/0005-2795(68)90230-4

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摘要: Abstract 1. (1)|The reaction of benzylpenicillin with various amines, amino acids and peptides in buffered aqueous solution at pH 7.4 was studied by means the penamaldate assay stability test. 2. (2)|In addition to e-aminogroups, α-aminogroups iminogroups proline, hydroxyl functions, e.g. present C-terminal serine, reacted benzylpenicillin. The penicilloylation N-terminal glycine oligoglycine is up ten times faster than e-amino function. presence a close second aminogroup on reacting molecule considerably accelerates formation penicilloylamides. 3. (3)|The guanidogroup arginine imidazole-function histidine do not react. N α - Z- dl -histidine slightly catalyzes hydrolysis benzylpenicilloic acid 9 11. 4. (4)|It concluded that rate depends functional group involved also neighbouring structure. Sites preferential proteins are be expected.

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