Evidence that platelet and skeletal sarcoplasmic reticulum Ca2+-ATPase are structurally distinct

Thomas H Fischer; Kevin P Campbell; Gilbert C White II

doi:10.1016/S0021-9258(17)39448-6

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Evidence that platelet and skeletal sarcoplasmic reticulum Ca2+-ATPase are structurally distinct

Journal article

Open access

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Evidence that platelet and skeletal sarcoplasmic reticulum Ca2+-ATPase are structurally distinct

Thomas H Fischer, Kevin P Campbell and Gilbert C White II

The Journal of biological chemistry, Vol.260(15), pp.8996-9001

1985

DOI: 10.1016/S0021-9258(17)39448-6

PMID: 3160695

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Abstract

Proteolytic digestion and indirect immunostaining were used to compare the platelet and sarcoplasmic reticulum Ca2+-ATPase proteins. When the platelet and sarcoplasmic reticulum Ca2+-ATPase proteins were digested in the native state with trypsin, the platelet Ca2+-ATPase, which had an apparent undigested molecular mass of 103 kDa, yielded 78-kDa and 25-kDa fragments. Calcium transport activity depended on the integrity of the 103-kDa protein, while the digested protein had residual ATPase activity. Tryptic digestion of the sarcoplasmic reticulum pump protein, which also had an undigested molecular mass of 103 kDa, yielded products with apparent molecular masses of 55 kDa, 36 kDa, and 26 kDa. Distinct patterns were also observed when the platelet and sarcoplasmic reticulum calcium pump proteins were digested with chymotrypsin and Staphylococcus aureus protease in the presence of sodium dodecyl sulfate. Chymotrypsin digestion of the platelet protein resulted in the appearance of products with apparent molecular masses of 70 kDa, 39 kDa, and 31 kDa, while a similar digestion of the sarcoplasmic reticulum calcium pump protein yielded 54-kDa, 52.5-kDa, 46-kDa, 41-kDa, and 36-kDa fragments. Exposure of the sarcoplasmic reticulum and platelet Ca2+-ATPase proteins to S. aureus protease also yielded dissimilar fragmentation patterns. These results indicate that the Ca2+-ATPases from platelets and sarcoplasmic reticulum are distinct proteins

Fundamental and applied biological sciences. Psychology

Biological and medical sciences

Hydrolases

Analytical, structural and metabolic biochemistry

Enzymes and enzyme inhibitors

Details

Title: Subtitle: Evidence that platelet and skeletal sarcoplasmic reticulum Ca2+-ATPase are structurally distinct
Creators: Thomas H Fischer - Univ. North Carolina, dep. medicine
Kevin P Campbell - Univ. North Carolina, dep. medicine
Gilbert C White II - Univ. North Carolina, dep. medicine
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.260(15), pp.8996-9001
DOI: 10.1016/S0021-9258(17)39448-6
PMID: 3160695
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology; Bethesda, MD
Language: English
Date published: 1985
Academic Unit: Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
Record Identifier: 9984068262002771

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