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Functional studies of single-site variants in the calmodulin-binding domain of RC3/neurogranin in Xenopus oocytes

✍ Scribed by J.B. Watson; J.E. Margulies; P.M. Coulter II; D.D. Gerendasy; J.G. Sutcliffe; R.W. Cohen


Book ID
117475119
Publisher
Elsevier Science
Year
1996
Tongue
English
Weight
366 KB
Volume
219
Category
Article
ISSN
0304-3940

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Role of Lys 558 and Lys 869 in substrate
✍ P. G. Wood; H. MΓΌller; M. Sovak; H. Passow πŸ“‚ Article πŸ“… 1992 πŸ› Springer 🌐 English βš– 888 KB

The effect of mutation of either Lys 558 or Lys 869 or both on mouse erythroid band 3 protein (AE1)-mediated 36Cl- efflux and its inhibition by pyridoxal 5-phosphate (P5-P), DNDS and H2DIDS were studied. Regardless of the mutation, band 3 was always capable of executing Cl- self-exchange. P5-P (5 mM