Abstract:
:cDNA clones encoding NADP(+)-glyceraldehyde-3-phosphate dehydrogenase (NADP(+)-GAPDH) and sedoheptulose-1,7-bisphosphatase (SBPase) were isolated and characterized from halotolerant Chlamydomonas sp. W80 (C. W80) cells. The cDNA clone for NADP(+)-GAPDH encoded 369 amino acid residues, preceded by the chloroplast transit peptide (37 amino acid residues). The cDNA clone for SBPase encoded 351 amino acids with the chloroplast transit peptide. The activities of NADP(+)-GAPDH and SBPase from C. W80 cells were resistant to H(2)O(2) up to 1 mM, as distinct from spinach chloroplastic thiol-modulated enzymes. The illumination to the dark-adapted cells and dithiothreitol treatment to the crude homogenate had little effect on the activities of NADP(+)-GAPDH and SBPase in C. W80. Modeling of the tertiary structures of NADP(+)-GAPDH and SBPase suggests that resistance of the enzymes to H(2)O(2) in C. W80 is due to the different conformational structures in the vicinity of the Cys residues of the chloroplastic enzymes between higher plant and C. W80 cells.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Tamoi M,Kanaboshi H,Miyasaka H,Shigeoka Sdoi
10.1006/abbi.2001.2375subject
Has Abstractpub_date
2001-06-15 00:00:00pages
176-85issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(01)92375-6journal_volume
390pub_type
杂志文章abstract::Existing literature describing the stoichiometry and stability of complexes between A23187 and divalent cations in solution has been extended to include additional transition series cations, the heavy-metal cations Cd2+ and Pb2+, plus seven lanthanide series trivalent cations. Stability constants of 1:1 complexes betw...
journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1999-04-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章,评审
doi:10.1016/j.abb.2008.10.025
更新日期:2009-04-15 00:00:00
abstract::Calcium-induced changes in protein solubility play a role in a variety of important biological processes including the deposition of bone and dentin and the secretion of milk. The phenomena of salt-induced (calcium) precipitation of proteins (salting-out), and the resolubilization of these proteins at higher salt conc...
journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1988-08-15 00:00:00