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Literature DB >> 133715

Molecular weights and hydrophobicity of the polypeptide chain of sarcoplasmic reticulum calcium(II) adenosine triphosphatase and of its primary tryptic fragments.

L J Rizzolo, M Maire, J A Reynolds, C Tanford.

Abstract

The polypeptide chain of the Ca2+-stimulated adenosine triphosphatase from sarcoplasmic reticulum has a molecular weight of 119 000+/-6500 on the basis of sedimentation equilibrium measurements in sodium dodecyl sulfate. The two primary fragments obtained by limited proteolysis each have within experimental error the same molecular weight, corresponding to one-half the molecular weight of the whole chain. Both fragments are eqaully resistant to complete denaturation by guanidine hydrochloride, a property characteristic of many intrinsic membrane proteins. This suggests that the native enzyme has two membrane-embedded halves, with an externally accessible link between them.

Entities: Chemical

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Year: 1976 PMID： 133715 DOI： 10.1021/bi00661a006

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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Cited

12 in total

1. Primary structures of cysteine-containing peptides from the calcium ion-transporting adenosine triphosphatase of rabbit sarcoplasmic reticulum.

Authors: G Allen; N M Green
Journal: Biochem J Date: 1978-08-01 Impact factor: 3.857

2. Gliding edge dislocations in proteins as a mechanism for active ion transport.

Authors: H D Chandler; C J Woolf; H R Hepburn
Journal: Biochem J Date: 1978-03-01 Impact factor: 3.857

3. Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis.

Authors: G G Hammes
Journal: Proc Natl Acad Sci U S A Date: 1982-11 Impact factor: 11.205

4. The primary structure of the calcium-transporting adenosine triphosphatase of rabbit skeletal sarcoplasmic reticulum. Soluble tryptic peptides from the succinylated carboxymethylated protein.

Authors: G Allen
Journal: Biochem J Date: 1980-06-01 Impact factor: 3.857

5. Mechanisms of integration of de novo-synthesized polypeptides into membranes: signal-recognition particle is required for integration into microsomal membranes of calcium ATPase and of lens MP26 but not of cytochrome b5.

Authors: D J Anderson; K E Mostov; G Blobel
Journal: Proc Natl Acad Sci U S A Date: 1983-12 Impact factor: 11.205

10. The reactivity of the thiol groups of the adenosine triphosphatase of sarcoplasmic reticulum and their location on tryptic fragments of the molecule.

Authors: D A Thorley-Lawson; N M Green
Journal: Biochem J Date: 1977-12-01 Impact factor: 3.857

Molecular weights and hydrophobicity of the polypeptide chain of sarcoplasmic reticulum calcium(II) adenosine triphosphatase and of its primary tryptic fragments.

1. Primary structures of cysteine-containing peptides from the calcium ion-transporting adenosine triphosphatase of rabbit sarcoplasmic reticulum.

2. Gliding edge dislocations in proteins as a mechanism for active ion transport.

3. Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis.

4. The primary structure of the calcium-transporting adenosine triphosphatase of rabbit skeletal sarcoplasmic reticulum. Soluble tryptic peptides from the succinylated carboxymethylated protein.

5. Mechanisms of integration of de novo-synthesized polypeptides into membranes: signal-recognition particle is required for integration into microsomal membranes of calcium ATPase and of lens MP26 but not of cytochrome b5.

Review 6. The sarcoplasmic reticulum Ca2+-ATPase.

Review 7. Calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of phospholamban.

8. 31P nuclear magnetic resonance studies of the phospholipid-protein interface in cell membranes.

9. Evidence for the influence of the protein-phospholipid interface on sarcoplasmic reticulum Ca++ Mg++ ATPase activity.

10. The reactivity of the thiol groups of the adenosine triphosphatase of sarcoplasmic reticulum and their location on tryptic fragments of the molecule.