Human prostate-specific antigen: structural and functional similarity with serine proteases.

@article{Watt1986HumanPA,
  title={Human prostate-specific antigen: structural and functional similarity with serine proteases.},
  author={K. W. K. Watt and Pyeong Jae Lee and T M'Timkulu and Wai-kong Chan and Rueyming Loor},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1986},
  volume={83 10},
  pages={3166-70}
}
The complete amino acid sequence of the prostate-specific antigen (PA) from human seminal plasma has been determined from analyses of the peptides generated by cyanogen bromide, hydroxylamine, endoproteinases Arg-C and Lys-C. The single polypeptide chain of PA contains 240-amino acid residues and has a calculated Mr of 26,496. An N-linked carbohydrate side chain is predicted at asparagine-45, and O-linked carbohydrate side chains are possibly attached to serine-69, threonine-70, and serine-71… CONTINUE READING
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