ライフサイエンスコーパス: zeta-crystallin

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1 ompeted with NADPH, the specific cofactor of zeta-crystallin.

2 o acid sequences showed that the protein was zeta-crystallin.

3 ione-S-transferases, superoxide dismutase 1, zeta crystallin, a NADPH quinone reductase, as well as g

4 zeta-Crystallin, a major cytosolic protein of guinea pig

5 did not affect this characteristic of bovine zeta-crystallin and the enzyme showed no binding affinit

6 t were identical to sequences found in mouse zeta-crystallin and three peptides that differed by only

7 On the other hand, bovine lens zeta-crystallin, but not guinea pig zeta-crystallin, sho

8 Furthermore, specific antibodies to zeta-crystallin, but not TIAR, blocked the formation of

9 egates contained alphaA-, beta-, gamma-, and zeta-crystallins, but not alphaB-crystallin, which is de

10 While the bovine lens zeta-crystallin exhibits similar physicochemical propert

11 vation of the alphaB-, alphaA-, delta1-, and zeta-crystallin genes in the lens.

12 Zeta-Crystallin is a taxon-specific crystallin, an enzym

13 eactivity with the guinea pig and human lens zeta-crystallins, it shows minimal quinone oxidoreductas

14 Thus, zeta-crystallin/NADPH:quinone reductase is a pH response

15 AR neither bound nor affected the binding of zeta-crystallin/NADPH:quinone reductase to the pH RE.

16 alysis were used to identify this protein as zeta-crystallin/NADPH:quinone reductase.

17 nine and having 62.2 and 62.9% identity with zeta-crystallin of camel and guinea pig lenses, respecti

18 Analysis of cDNA sequence encoding zeta-crystallin of the tree frog lens demonstrated that

19 ed structure was calculated to be 35,564 Da. zeta-Crystallin of the tree frog lens exhibited the intr

20 All zeta-crystallin present in the nuclear WI fraction appea

21 to Nrl, and cotransfection with Nrl elevates zeta-crystallin promoter activity in lens cells.

22 TvQR1 is a member of the zeta-crystallin quinone oxidoreductase family that catal

23 Alignment of eight zeta-crystallin sequences, and computer modelling of the

24 o-dimensional electrophoresis of bovine lens zeta-crystallin showed a distinct pattern of posttransla

25 ine lens zeta-crystallin, but not guinea pig zeta-crystallin, showed a strong binding affinity to sin

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