Improved Separation of Lm (Low Molecular Weight) Crystallins
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Publisher
Springer Netherlands
Link
http://link.springer.com/content/pdf/10.1007/978-94-010-1571-4_10.pdf
Reference25 articles.
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2. Björk, I. Studies on γ-crystallin from calf lens. II. Purification and some properties of the main protein components. Exp. Eye Res. 3: 254–261 (1964).
3. Bloemendal, H. Zone Electrophoresis in Blocks and Columns. Elsevier Publishing Company; Elsevier Monographs: Chemistry Section 28 (1963).
4. Bloemendal, H. Alpha-crystallin. Structural aspects and biosynthesis. Acta Morphol Neerl-Scand. 10: 197–213 (1972).
5. Bloemendal, H., A.J.M. Berns, F. Van Der Ouderaa & W.W.W. De Jong. Evidence for a ‘non-genetic’ origin of the A1 chain of α-crystallin. Exp. Eye Res. 14: 80–81 (1972a).
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3. Comparative studies of βs-crystallins from human, bovine, rat and rabbit lenses;Current Eye Research;1989-01
4. Further studies on low molecular weight crystalline: Relationship between the bovine βSthe human 24kD protein and the γ-crystallins;Current Eye Research;1986-01
5. A second polymorphic lens crystallin (LEN-2) in the mouse: Genetic and biochemical analysis of LEN-1 and LEN-2;Biochemical Genetics;1985-02
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