TY - JOUR
T1 - ζ-Crystallin is a major protein in the lens of Camelus dromedarius
AU - Garland, Donita
AU - Rao, P. Vasantha
AU - Corso, Antonella Del
AU - Mura, Umberto
AU - Zigler, J. Samuel
PY - 1991/2/15
Y1 - 1991/2/15
N2 - 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.
AB - 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.
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U2 - 10.1016/0003-9861(91)90339-K
DO - 10.1016/0003-9861(91)90339-K
M3 - Article
C2 - 1990971
AN - SCOPUS:0026034018
SN - 0003-9861
VL - 285
SP - 134
EP - 136
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -