Two human trypsinogens. Purification, molecular properties, and N-terminal sequences.

@article{Guy1978TwoHT,
  title={Two human trypsinogens. Purification, molecular properties, and N-terminal sequences.},
  author={O Guy and Dominique Lombardo and Diana C Bartelt and J. Amic and Catherine Figarella},
  journal={Biochemistry},
  year={1978},
  volume={17 9},
  pages={1669-75}
}
The two human trypsinogens have been isolated from human pancreatic juice in a sufficient amount to study molecular and structural properties. The purification procedure included filtration on Sephadex G-100 followed by ion-exchange chromatography on DEAE-cellulose. The two trypsinogens represent 19% of total proteins of pancreatic juice. Trypsinogen 1, the major form, is present in a quantity twice that of trypsinogen 2, which is the most anionic protein in human pancreatic juice. The two… CONTINUE READING

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