The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure.

@article{Wen1996ThePA,
  title={The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure.},
  author={Dingyi Wen and K Corina and E. Pingchang Chow and Stephan K Miller and Paul A. Janmey and Robert Blake Pepinsky},
  journal={Biochemistry},
  year={1996},
  volume={35 30},
  pages={9700-9}
}
Gelsolin is a widely distributed actin binding protein that regulates actin filament length. It exists in both an intracellular and an extracellular form that is derived from a single gene by alternative splicing. Both forms contain the six homologous domains that are responsible for function. Little is known regarding differences between the forms. We have used a combination of cysteine-specific modification with 4-vinylpyridine, HPLC peptide mapping methods, and mass spectrometry to analyze… CONTINUE READING

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