three are heat resistant. There is no relationship between migration and. heat sensitivity. These findings indicate that mycobacterial catalases are present in multiple molecular forms. All of these forms appear to have a lower molecular weight than the previously studied mammalian and bacterial ca
Lysine oligopeptides. Preparation by ion-exchange chromatography
โ Scribed by A. Yaron; M. C. Otey; H. A. Sober; E. Katchalski; S. Ehrlich-Rogozinski; A. Berger
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1972
- Tongue
- English
- Weight
- 727 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0006-3525
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โฆ Synopsis
The preparation of L-lysine peptides (Lys,, n = 2-14) from poly-L-lysine is described.
Fractionation by ion-exchange column chromatography of poly-Llysine hydrolysates on apreparative scale resulted in 0.2-1.0g quantities of individual members of the poly-Llysine series. The peptides isolated proved to be analytically pure and the optical configuration was fully retained, as demonstrated by complete enzymic digestion. Peptides higher than n = 14 were also prepared. They cousist,ed of oligolysine groups of narrow and accurately determined size distribution. Potentiometric t.itratioris were used both to characterize the products and to demonstrate t.he charact~eristic dependence of the dissociation constants on size of the peptide.
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