Purification of neutral lens endopeptidase: close similarity to a neutral proteinase in pituitary.

@article{Ray1985PurificationON,
  title={Purification of neutral lens endopeptidase: close similarity to a neutral proteinase in pituitary.},
  author={Kaushik Ray and Harry Harris},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1985},
  volume={82 22},
  pages={7545-9}
}
A neutral endopeptidase (EC 3.4.24.5) that degrades alpha- and beta-crystallins occurs in mammalian lens. A procedure for purification of this enzyme from bovine lens is described. The enzyme appears to have a high molecular weight (Mr approximately equal to 700,000) and under denaturing conditions dissociates into at least eight polypeptide subunits with Mrs ranging from 24,000 to 32,000. A neutral proteinase in bovine pituitary has been reported previously to have similar structural… CONTINUE READING
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