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Fraktionierung der α-Keratose an gepufferten Sephadexsäulen

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Zusammenfassung

Aus Merino-Kammzug isolierteα-Keratose wurde mit Hilfe verschiedener Sephadex-Gele chromatographisch aufgetrennt. Die besten Trenneffekte konnten dabei mit Sephadex G 75 in 5 m langen Säulen unter Verwendung von schwach alkalischen Puffern erzielt werden; neben einer sehr heterogenen Hauptkomponenteα KA und einer in sehr geringer Konzentration vorhandenen Fraktionα KB1 wurde ein in Wolle zu 6% vorhandenes einheitliches Proteinα KB2 isoliert.

Nach Rechromatographie der Fraktionα KB2 wurde deren Molekulargewicht mit Hilfe der Ultrazentrifuge zu 8300 bestimmt. Dasα KB2-Protein wies alle auch in Wolle vorhandenen sieben N-terminalen Endgruppen, aber nur Tyrosin als C-terminale Endgruppe auf. Aminosäureanalysen zeigten einen hohen Gehalt der Aminosäuren Tyrosin, Phenylalanin und Glycin an.

Summary

α-keratose isolated from wool was fractionated by gelchromatography under optimum conditions — using Sephadex G 75 in 5 m columns and mild alkaline-buffered solutions of theα-keratose. Theα-keratose was separated into three main parts: a very heterogeneous component calledα KA protein, a very small fraction namedα KB1-protein and a pure proteinα 2KB (6% of total wool).

After rechromatography of theα KB2-fraction the molecular weight of the protein was estimated to be 8300. Analysis of the N-terminal endgroups showed that theα KB2-protein contains the same N-terminal amino acids as wool; but there is only one C-terminal amino acid (tyrosine). A very high content of tyrosine, phenylalanine and glycine was found by amino acid analysis of theα KB2-protein.

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Literatur

  1. Reithel, F. J., Advances Protein Chem.18, 124 (1963).

    Google Scholar 

  2. Blackburn, S. undA. G. Lowther, Biochem. J.49, 554 (1951);Zahn, H., H. G. Otten undK. Ateya, Textil Rdsch.19, 204 (1964);Leach, S. J., G. E. Rogers undB. K. Filshie, Arch. Biochem. Biophys.105, 270 (1964);Bradbury, J. H., G. V. Chapman undN. L. R. King, IIIe Congr. Int. Rech. Textile Lainière (Cirtel), Institut Textile de France Paris1, 359 (1965);Miro, P, undJ. Blade, IIIe Congr. Int. Rech. Textile Lainière (Cirtel), Institut Textile de France Paris1, 507 (1965).

    PubMed  Google Scholar 

  3. Crewther, W. G., J. M. Gillespie, B. S. Harrap, I. J. O'Donnell undE. O. P. Thompson, IIIe Congr. Int. Rech. Textile Lainière (Cirtel), Institut Textile de France Paris1, 475 (1965).

    Google Scholar 

  4. Crewther, W. G., R. D. B. Fraser, F. G. Lennox undH. Lindley, Advances Protein Chem.20, 191 (1965).

    PubMed  Google Scholar 

  5. Gillespie, J. M., Aust. J. Biol. Sci.13, 81 (1960);Gillespie, J. M. undF. G. Lennox, Biochim. Biophys. Acta12, 481 (1953);Gillespie, J. M., Biochim. Biophys. Acta27, 225 (1958).

    Google Scholar 

  6. Gillespie, J. M. undB. S. Harrap, Aust. J. Biol. Sci.16, 542 (1963).

    Google Scholar 

  7. O'Donnell, I. J. undE. O. P. Thompson, Aust. J. Biol. Sci.15, 746 (1962) und17, 973 (1964).

    Google Scholar 

  8. Corfield, M. C., Biochem. J.84, 602 (1962) und86, 125 (1963).

    Google Scholar 

  9. Fell, M., N. H. La France undK. Ziegler, J. Text. Inst.51, T 797 (1960).

    Google Scholar 

  10. Alexander, P. undL. Smith, Proc. Int. Wool Text. Res. Conf. Aust. 1955, B-58.

  11. Spackman, D. H., W. H. Stein undS. Moore, Anal. Chem.30, 1190 (1958).

    Google Scholar 

  12. Siepmann, E. undH. Zahn, IIIe Congr. Int. Rech. Textile Lainière (Cirtel), Institut Textile de France ParisI, 303 (1965).

    Google Scholar 

  13. Haylett, T., F. J. Joubert, L. S. Swart undD. F. Louw, Text. Res. J.33, 639 (1963).

    Google Scholar 

  14. Andrews, P., Nature196, 36 (1962).

    PubMed  Google Scholar 

  15. Andrews, P., Biochem. J.91, 222 (1963).

    Google Scholar 

  16. Moore, S. undW. H. Stein, J. Biol. Chem.211, 907 (1954).

    PubMed  Google Scholar 

  17. Sanger, F., Biochem. J.39, 507 (1945).

    Google Scholar 

  18. Middlebrook, W. R., Biochim. Biophys. Acta7, 547 (1951).

    PubMed  Google Scholar 

  19. Corfield, M. C., A. Robson undB. Skinner, Biochem. J.68, 348 (1958).

    PubMed  Google Scholar 

  20. Thompson, E. O. P., Aust. J. Biol. Sci.10, 225 (1957).

    Google Scholar 

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Author notes

  1. Marita Fell & Hans -Karl Rouette

    Present address: Deutschen Wollforschungsinstitut Aachen, Deutschland

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    1. Marita Fell
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    2. Hans -Karl Rouette
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    4. Mitteilung über Untersuchungen anα-Keratose. 3. MitteilungM. Fell, Kolloid-Z. u. Z. Polymere220, 107 (1967).

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    Fell, M., Rouette, H.K. Fraktionierung der α-Keratose an gepufferten Sephadexsäulen. Kolloid-Z.u.Z.Polymere 222, 103–110 (1968). https://doi.org/10.1007/BF01510791

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