Secondary structure of the Neurospora crassa plasma membrane H+-ATPase as estimated by circular dichroism.
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چکیده
منابع مشابه
The fluorescein isothiocyanate-binding site of the plasma-membrane H+-ATPase of Neurospora crassa.
The mammalian (Na+,K+), Ca2+-, and (H+,K+)-ATPases contain a well-characterized lysine residue that reacts with fluorescein 5'-isothiocyanate (FITC); enzymatic activity is protected by ATP, suggesting that the residue is located in or near the nucleotide-binding domain. In this study, the plasma-membrane H+-ATPase of Neurospora crassa is also shown to be sensitive to FITC. The reaction occurs w...
متن کاملChemical state of the cysteine residues in the Neurospora crassa plasma membrane H(+)-ATPase.
The plasma membrane H(+)-ATPase of Neurospora crassa was treated with 5,5'-dithiobis(2-nitrobenzoate) to determine its cysteine content and with 2-nitro-5-thiosulfobenzoate to determine its cystine content. Six and seven mol of thiols/mol of H(+)-ATPase were detected in the 5,5'-dithiobis(2-nitrobenzoate) and 2-nitro-5-thiosulfobenzoate reactions, respectively, indicating that 6 of the 8 cystei...
متن کاملModification of the Neurospora crassa plasma membrane [H+]-ATPase with N,N'-dicyclohexylcarbodiimide.
The [H+]-ATPase of the Neurospora plasma membrane is composed of a single Mr = 104,000 polypeptide (B. J. Bowman, F. Blasco, and C. W. Slayman, J. Biol. Chem. (1981) 256, 12343-12349). The carboxyl-modifying reagent N,N'-dicyclohexylcarbodiimide (DCCD) inactivates the ATPase with pseudo-first order kinetics, suggesting that one site on the enzyme is involved. The rate constant for inactivation ...
متن کاملLocation of a dicyclohexylcarbodiimide-reactive glutamate residue in the Neurospora crassa plasma membrane H+-ATPase.
The proton pump (H+-ATPase) found in the plasma membrane of the fungus Neurospora crassa is inactivated by dicyclohexylcarbodiimide (DCCD). Kinetic and labeling experiments have suggested that inactivation at 0 degrees C results from the covalent attachment of DCCD to a single site in the Mr = 100,000 catalytic subunit (Sussman, M. R., and Slayman, C. W. (1983) J. Biol. Chem. 258, 1839-1843). I...
متن کاملSolubilization and purification of the Neurospora plasma membrane H+-ATPase.
The electrogenic proton-translocating ATPase in the plasma membrane of Neurospora has been solubilized with lysolecithin and purified using a combination of gel filtration and density gradient centrifugation. Isolated plasma membrane vesicles are solubilized with lysolecithin in the presence of MgATP, vanadate, and chymostatin. The MgATP and vanadate are required to maintain the ATPase in an ac...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)69044-1