| Literature DB >> 1990971 |
D Garland1, P V Rao, A Del Corso, U Mura, J S Zigler.
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 zeta-crystallin and peptides corresponding to amino acids 1-10 and 295-308, but not to antibodies raised against amino acids 320-328 of zeta-crystallin. Based on these criteria it is concluded that this protein, which is a major constituent of camel lens, is zeta-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.Entities:
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Year: 1991 PMID: 1990971 DOI: 10.1016/0003-9861(91)90339-k
Source DB: PubMed Journal: Arch Biochem Biophys ISSN: 0003-9861 Impact factor: 4.013