Abstract:
:The sarcoplasmic reticulum (SR) membranes of rabbit skeletal muscle were allowed to react with N-(3-pyrene)maleimide (PMI) at pH 7 at 30 degrees C. The Ca(2+)-transporting activity of the SR membranes was reduced to 20% when PMI was bound to the extent of 1 mol/mol of Ca(2+)-transporting ATPase. The ATPase and the E-P forming activities were not affected by the binding of PMI up to 2 mol/mol ATPase, indicating that PMI somehow uncoupled Ca(2+)-transport from ATP splitting. Permeability of the SR membranes to Ca2+ ions was increased in parallel with the loss of the Ca(2+)-transporting activity. Of several components of the SR membranes which are reactive with PMI, the ATPase protein was the only one whose modification by PMI was directly related to the loss of the Ca(2+)-transporting activity. Similar results were obtained with the light SR membrane fraction, which lacks the ryanodine receptor, a well-recognized Ca2+ channel. These results indicated that a Ca2+ channel that would have been latent or properly regulated in native ATPase somehow escaped from the normal control mechanism as a result of modification of its SH groups by PMI and went into runaway operation. The activated channel was specific for alkaline earth metal ions, so permeability to other solutes including Co2+, Ni2+, and sucrose remained unchanged after treatment with PMI.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Suzuki T,Kawakita Mdoi
10.1093/oxfordjournals.jbchem.a124155subject
Has Abstractpub_date
1993-08-01 00:00:00pages
203-9issue
2eissn
0021-924Xissn
1756-2651journal_volume
114pub_type
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更新日期:1976-05-01 00:00:00
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pub_type: 杂志文章
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更新日期:1992-04-01 00:00:00
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a134406
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pub_type: 杂志文章
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更新日期:2012-05-01 00:00:00
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pub_type: 杂志文章
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更新日期:1977-05-01 00:00:00
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更新日期:2001-06-01 00:00:00
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更新日期:2005-12-01 00:00:00