10.1111/j.1432-1033.1989.tb14806.x
Crossref journal-article
Wiley
European Journal of Biochemistry (311)
Abstract

From the analysis of phylogenetic trees constructed from the amino acid sequences and metal‐binding properties of various lysozymes c and α‐lactalbumins, it was found that before the divergence of the lineages of birds and mammals, calcium‐binding lysozyme diverged from non‐calcium‐binding lysozyme. α‐Lactalbumin evolved from the calcium‐binding lysozyme along the mammalian lineage after the divergence of birds and mammals. Rapid evolution took place, not in the process of acquisition of the activity of α‐lactalbumin, but after the loss of lysozyme activity, due to the change in the distribution of selective pressure on each amino acid site.A general process for the change in function of a protein during evolution is suggested to be as follows: after duplication of the gene, one of their protein products acquires a new function, besides that already present; the old function is eventually lost.

Bibliography

NITTA, K., & SUGAI, S. (1989). The evolution of lysozyme and α‐lactalbumin. European Journal of Biochemistry, 182(1), 111–118. Portico.

Authors 2
  1. Katsutoshi NITTA (first)
  2. Shintaro SUGAI (additional)
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Dates
Type When
Created 20 years, 5 months ago (March 3, 2005, 10:09 p.m.)
Deposited 1 year, 9 months ago (Oct. 31, 2023, 8:59 a.m.)
Indexed 1 month, 2 weeks ago (July 4, 2025, 7:48 a.m.)
Issued 36 years, 2 months ago (June 1, 1989)
Published 36 years, 2 months ago (June 1, 1989)
Published Online 20 years, 5 months ago (March 3, 2005)
Published Print 36 years, 2 months ago (June 1, 1989)
Funders 0

None

@article{NITTA_1989, title={The evolution of lysozyme and α‐lactalbumin}, volume={182}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1989.tb14806.x}, DOI={10.1111/j.1432-1033.1989.tb14806.x}, number={1}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={NITTA, Katsutoshi and SUGAI, Shintaro}, year={1989}, month=jun, pages={111–118} }