Advances in Protein Chemistry, 8 by M L Anson; J T Edsall

By M L Anson; J T Edsall

ADVANCES IN PROTEIN CHEMISTRY VOL 8.

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For the extraction of the peptide, the medium is saturated with ammonium sulfate and extracted with isopropyl alcohol. The peptide is adsorbed from the isopropyl solution on to alumina, and then eluted into water. It ia then precipitated from aqueous solution with picric acid. The polymyxin picrate is converted to the hydrochloride derivative from which it undergoes further purification (475,522). By saturation with ammonia (55) the free base can be precipitated from a concentrated aqueous solution of the hydrochloride.

558) noted that chicken pancreas conjugase is inhibited by p-aminobenzoyltriglutamic acid, and Sims and Totter (528) observed this to be true for yeast p-amiiiobenzoylpolyglutamic acid, which also inhibits rat NATURALLY OCCURRING PEPTIDER 49 liver conjugase in vitro. The action of this polypeptide on pig kidney conjugase is not known. Mims, Swendseid, and Bird (417) have shown that deoxy- and ribonucleic acids are powerful inhibitors of pig kidney and intestinal conjugases. The inhibitory effect of these nucleic acids disappears after they have been acted upon by ribonuclease or deoxyribonucleodepolymerase.

The identity of the naturally occurring substance and the synthetic peptide has been confirmed by a comparison of their infrared (82)and ultraviolet (83) spectra. (3) Pteroylheptaglutamic Acid. The structure of the vitamin B, conjugate is not yet entirely clear. Pfiffner el al. (462) from ultraviolet absorption spectra data believe that this conjugate is built up of vitamin B, linked with a lateral, nonultraviolet-absorbing, nitrogen-containing chain. Acid hydrolysis of the conjugate (461) liberates 7 moles of L ( + ) glutamic acid for each mole of p-aminobenzoic acid.

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