Abstract
Camel (Camelus dromedarius) lenses contain a protein with an apparent subunit Mr 38,000 that constitutes approximately 8-13% of the total protein. The protein has been purified and has a native Mr 140,000 as determined by gel filtration. This is consistent with its being a tetramer. The protein reacts with antibodies raised against both guinea pig ζ-crystallin and peptides corresponding to amino acids 1-10 and 295-308, but not to antibodies raised against amino acids 320-328 of ζ-crystallin. Based on these criteria it is concluded that this protein, which is a major constituent of camel lens, is ζ-crystallin. This may be the first example of a protein (enzyme) being independently utilized as a crystallin in the lens of species from two mammalian orders.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 134-136 |
| Number of pages | 3 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 285 |
| Issue number | 1 |
| DOIs | |
| State | Published - Feb 15 1991 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
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