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Study

Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish

Chen, Liangbiao; DeVries, Arthur L.; Cheng, Chi-Hing C.

Proceedings of the National Academy of Sciences, 1997

Peer-reviewedgenomic studylaboratory

Sequenced the antifreeze glycoprotein gene and compared it with the genome, identifying the ancestral gene it derived from and the structural changes involved.

Studied in
Notothenioidei
Sample size
gene and genomic sequence comparison

The antifreeze glycoprotein gene evolved from a pancreatic trypsinogen gene — a digestive enzyme — by amplification of a short repeated segment, with parts of the ancestral gene still recognisably present.

What it means

The authors' reading, and ours. Where they differ, that difference is the point.

How the authors put it

A new protein with an entirely new function arose by co-option and internal duplication from an existing gene, and the intermediate stages are still readable in the sequence.

How NatureHQ reads it

The clearest molecular case NatureHQ has for the point the adaptation page makes in the abstract: survival machinery is frequently recruited rather than invented. A digestive enzyme became an antifreeze, and the paperwork survived.

  • Sequence evidence for an ancestral relationship is inference from similarity, though here the similarity is unusually clear.
  • The selective conditions under which the transition occurred are reconstructed rather than observed.

What this study is used for on NatureHQ

One study can inform several subjects. Here is everywhere this one is cited.

Published by: Proceedings of the National Academy of SciencesPublished in PNAS.

doi.org/10.1073/pnas.94.8.3811

Checked against Crossref on 2026-09-28, and they agree on the title, the authors and the year.

NatureHQ summarises research in its own words and does not reproduce published text. Reviewed 2026-09-03.