57 pp.
57 pp.
| 1798 K 57 pp. | |
| View Document | ||
| Title | Occurrence and Characteristics of a Rapid Exchange of Phosphate Oxygens Catalyzed by Sarcoplasmic Reticulum Vesicles | |
| Author(s) | Kanazawa, T.; Boyer, P. D. | |
| Publication Date | 1972 | |
| Report Number | UCLA--34-P-102-35 | |
| Unique Identifier | ACC0192 | |
| Other Numbers | OSTI ID: 4473783 | |
| Research Org | University of California, Los Angeles (USA) | |
| Contract No | AT(04-3)-34 | |
| Sponsoring Org | U.S. Atomic Energy Commission (AEC) | |
| Subject | 06 Biomed; 07 Chemistry; Animal Cells -- Respiration; ATP-ASE; Biochemical Reaction Kinetics; Calcium; Catalysts; Endoplasmic Reticulum; Magnesium; Metabolism; Muscles; Oxygen; Phosphates; Rabbits; Water | |
| Related Web Pages | Paul D. Boyer, Adenosine Triphosphate [ATP], and the Binding Change Mechanism | |
| Abstract | Sarcoplasmic reticulum vesicles isolated from skeletal muscle actively take up Ca{sup ++} from the medium in the presence of Mg{sup ++} and ATP. This transport is coupled to ATP hydrolysis catalyzed by membrane-bound Ca{sup++}, Mg{sup ++}-ATPase which is activated by concurrent presence of Ca{sup ++} and Mg{sup ++}. Considerable informations have accumulated that give insight into the ATPase and its coupling to the calcium transport. The hydrolysis of ATP by this enzyme occurs through a phosphorylated intermediate. Formation and decomposition of the intermediate show vectorial requirements for Ca{sup ++} and Mg{sup ++}, suggesting an intimate involvement of the intermediate in the transport process. ATP synthesis from P{sub i} and ADP coupled to outflow of Ca{sup ++} from sarcoplasmic reticulum vesicles has recently been demonstrated. This indicates the reversibility of the entire process of calcium transport in sarcoplasmic reticulum vesicles. | |
| 1798 K 57 pp. | |
| View Document | ||
