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Journal ArticleDOI

Hydrolysis by horse muscle acylphosphatase of (Ca2+ + Mg2+)-ATPase phosphorylated intermediate.

TLDR
Findings suggest a possible regulatory role of this enzyme in vivo on the calcium transport process by sarcoplasmic reticulum by way of acylphosphatase in rabbit muscle.
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This article is published in Archives of Biochemistry and Biophysics.The article was published on 1981-04-15. It has received 29 citations till now. The article focuses on the topics: Acylphosphatase & Ca(2+) Mg(2+)-ATPase.

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Citations
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Journal ArticleDOI

Conformational constraints for amyloid fibrillation: the importance of being unfolded.

TL;DR: In this review, recent findings are surveyed to illustrate that protein fibrillogenesis requires a partially folded conformation, which is relatively unfolded, and shares many structural properties with the pre-molten globule state.
Journal ArticleDOI

Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH.

TL;DR: The results indicate that acylphosphatase is a relatively unstable protein with a delta G(H2O) of 22 +/- 1 kJ mol-1 at pH 7 and 25 degrees C, suggesting that the overall dimensions of the unfolded state are significantly affected by the number of charges within the polypeptide chain.
Journal ArticleDOI

A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure.

TL;DR: A new acylphosphatase from human erythrocytes was isolated by an original purification procedure, and it was found to differ in 44% of the total positions as compared to the human muscle enzyme.
Journal ArticleDOI

Effects of acylphosphatase on the activity of erythrocyte membrane Ca2+ pump.

TL;DR: Findings suggest that, because of its hydrolytic activity on the phosphoenzyme intermediate, acylphosphatase reduces the efficiency of the erythrocyte membrane Ca2+ pump.
Journal ArticleDOI

Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Thr42, and Thr46.

TL;DR: The reported results strongly support a direct participation of Asn41 to the enzyme catalytic mechanism, indicating that Asn 41 mutants may well represent a useful tool for the investigation of the enzyme physiological function by the negative dominant approach.
References
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Journal ArticleDOI

A Borohydride Reduction Method for Characterization of the Acyl Phosphate Linkage in Proteins and Its Application to Sarcoplasmic Reticulum Adenosine Triphosphatase

TL;DR: The results demonstrate that the phosphoryl group of sarcoplasmic reticulum ATPase is attached to the β-carboxyl group of an aspartyl residue at the active site.
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Sarcoplasmic reticulum. VII. Properties of a phosphoprotein intermediate implicated in calcium transport.

TL;DR: Hydrolysis of 32P-labeled adenosine triphosphate by skeletal muscle microsomes occurs through a protein-bound phosphate intermediate, which is probably an acyl phosphate.
Journal ArticleDOI

Studies on the Location and Orientation of Proteins in the Sarcoplasmic Reticulum

TL;DR: The adenosine triphosphatase of sarcoplasmic reticulum has been split into three parts by digestion with trypsin and it is suggested that the 60000-mol.
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Structural and chemical asymmetry of the calcium-transporting membranes of the sarcotubular system as revealed by electron microscopy.

TL;DR: In experiments where the vesicles were incubated with the SH-reagent Hg-phenyl azoferritin, a close packing of ferritin particles at the outer surface of thevesicular membrane was observed, interpreted as indicating a preferred localization of the active sites involved in the calcium transport at theoutersurface of the membrane.
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