Publication: Different states of sarcoplasmic reticulum membrane in the presence of acetyl phosphate and adenosine triphosphate
2
Issued Date
1977-09-01
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ISSN
00243205
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2-s2.0-0017657821
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Mahidol University
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SCOPUS
Bibliographic Citation
Life Sciences. Vol.21, No.5 (1977), 713-718
Suggested Citation
Yongyuth Yuthavong, Pailin Ucchin, Rossukon Sari Different states of sarcoplasmic reticulum membrane in the presence of acetyl phosphate and adenosine triphosphate. Life Sciences. Vol.21, No.5 (1977), 713-718. doi:10.1016/0024-3205(77)90080-7 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/10234
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Title
Different states of sarcoplasmic reticulum membrane in the presence of acetyl phosphate and adenosine triphosphate
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Abstract
In the presence of acetyl phosphate, approximately 0.8 extra sulphydryl groups/10 5 g protein of sarcoplasmic reticulum membrane vesicles are exposed to reaction with N-ethylmaleimide, whereas in the presence of ATP approximately 0.6 groups/10 5 g protein are protected. Dithiobis (nitrobenzoic acid) reacts with the membrane sulphydryl groups more slowly in the presence of ATP than in the presence of acetyl phosphate or in the absence of substrate. Sarcoplasmic reticulum membrane is degraded by trypsin at a faster rate than normal when acetyl phosphate is present as seen from changes in electrophoretic patterns, ATPase activity and Ca 2+ uptake capacity, and at a slower rate when ATP is present as seen from the last two properties. These differences in reactivity are interpreted as being due to differences in membrane conformations induced by the two substrates. © 1977.