N-Terminal Amino-acids of Bovine Eye Lens Proteins

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Abstract

THE proteins of the crystalline lens are of particular significance to the embryologist because of the (serological) organ specificity of this part of the eye. In connexion with other biochemical and serological studies in our laboratory an investigation is being made on the N-terminal amino-acids of the main lens proteins : α-, β- and γ-crystallin. The preparations of α-crystallin have been isolated mainly by zone electrophoresis on starch1. They showed one single peak in both paper electrophoresis and moving-boundary electrophoresis at pH. 4.2; 6.2; 7.1; 7.8; and 8.9 respectively. In the ultracentrifuge only a very small percentage of impurities was still noticeable. Some preliminary experiments were also made on β- and γ-crystallin, which preparations were obtained by salting out with ammonium sulphate and still showed small amounts of impurities when investigated by electrophoresis and ultracentrifugation.

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References

  1. 1

    Bloemendal, H., Proc. Kon. Ned. Akad. Wet., C, 59, 22 (1956).

  2. 2

    Fraenkel-Conrat, H., Harris, J. I., and Levy, A. L., in “Methods of Biochemical Analysis”, edit. by Glick, D., 2, 360 (New York, 1955).

  3. 3

    Levy, A. L., Nature, 174, 126 (1954).

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BLOEMENDAL, H., CATE, G. N-Terminal Amino-acids of Bovine Eye Lens Proteins. Nature 181, 340–341 (1958) doi:10.1038/181340a0

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