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• W2008470913 abstract "Argininosuccinate lyase (ASL)/δ-crystallin, a major soluble protein of the transparent eye lens of birds and reptiles, is a mixture of tetramers comprising all possible combinations of two similar polypeptides (δ1 and δ2). Only the δ2 polypeptide has ASL activity. In the present investgation we have purified each of the 5 major isoforms (δA to δE, pI 5.2 to 5.8) of δ-crystallin tetramers from the embryonic duck lens by isoelectric focussing and established by peptide sequencing that the δ1 and δ2 polypeptides are encoded in the previously identified, linked δ1 and δ2 genes, respectively. The relative amounts of the different tetramers in the 14-day-old embryonic lens were consistent with equal expression of the 2 δ-crystallin genes and no preference for assembly of the 2 δ polypeptides. The relative amount of ASL activity of the tetramers was a linear function of the relative amount of their δ2 polypeptides, with δA (only δ1) lacking enzymatic activity altogether. δB (3 δ1:1 δ2), δC (2 δ1:2 δ2), δD (1 δ1:3 δ2) and δE (4 δ2) all gave normal Michaelis-Menten kinetics for fumarate production from argininosuccinate at 40°C and had a similar Km (average Km for mixture was 0.15 mM). δE had a Km of 0.187 mM and a Vmax of 9 μmol/min per mg protein. Unlike bovine and like human ASL, both reported previously, embryonic duck ASL/δ-crystallin showed no evidence of cooperativity or activation by GTP. Each isoform had a similar far ultraviolet circular dichroism spectrum and thermal stability between 20°C and 60°C, with denturation occurring at 65°C. Our data suggest that gene duplication, structural modifications leading to greater thermal stability of the δ1 and δ2 polypeptides, and selective loss of ASL activity in the δ1 polypeptide all occurred during the recruitment of ASL for a refractive role in the duck lens, resulting in the generation of ASL isoenzymes." @default.
• W2008470913 created "2016-06-24" @default.
• W2008470913 creator A5031937602 @default.
• W2008470913 creator A5067297656 @default.
• W2008470913 date "1996-07-01" @default.
• W2008470913 modified "2023-10-03" @default.
• W2008470913 title "Characterization and enzyme activity of argininosuccinate lyase/δ-crystallin of the embryonic duck lens" @default.
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• W2008470913 doi "https://doi.org/10.1016/0167-4838(96)00030-1" @default.
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• W2008470913 hasPublicationYear "1996" @default.
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