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Aggregation behavior of the bovine β-crystallin Bp chain studied by limited proteolysis

  • Published:1983-10 Issue:2 Volume:748 Page:213-219
  • ISSN:0167-4838
  • Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
  • language:en
  • Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Berbers Guy A.M.,Brans Annemoon M.M.,Hoekman Willeke A.,Slingsby Christine,Bloemendal Hans,De Jong Wilfried W.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Cited by 33 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Solution conformation of bovine lens α-and βB2-crystallin terminal extensions;International Journal of Peptide and Protein Research;2009-01-12

2. Identification of the Primary Targets of Carbamylation in Bovine Lens Proteins by Mass Spectrometry;Current Eye Research;2008-01

3. Rapid purification of recombinant βB2-crystallin using hydrophobic interaction chromatography;Protein Expression and Purification;2003-03

4. βB2-crystallin undergoes extensive truncation during aging in human lenses;Biochemical and Biophysical Research Communications;2003-01

5. Formation of βA3/βB2-crystallin mixed complexes: involvement of N- and C-terminal extensions;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1999-07
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