P-31 NMR-STUDIES OF THE ATP ALPHA-CRYSTALLIN COMPLEX - FUNCTIONAL IMPLICATIONS

被引：44

作者：

REDDY, MC ^{[1
]}

PALMISANO, DV ^{[1
]}

GROTHVASSELLI, B ^{[1
]}

FARNSWORTH, PN ^{[1
]}

机构：

[1] UMD, NEW JERSEY MED SCH, DEPT OPHTHALMOL, NEWARK, NJ 07103 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 189卷 / 03期

关键词：

D O I：

10.1016/0006-291X(92)90256-K

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Evidence is presented for the binding of ATP to α-crystallin in the lens by 31P NMR spectroscopic measurements. The chemical shift data as well as the T1 and T2 values indicate that Pβ and Pγ of ATP are of prime importance in binding. In addition, it is demonstrated that the association of α-crystallin with purified fiber cell membranes is significantly enhanced by the addition of ATP. These results suggest that ATP modulates the functional behavior of α-crystallin. © 1992.

引用

页码：1578 / 1584

页数：7

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