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- W1987550340 abstract "Abstract It has been shown that the proteins present in the membranes of sarcoplasmic reticulum microsomes isolated from rabbit skeletal muscle are susceptible to trypsin digestion. When digestion was carried out in 10 m m imidazole, pH 7.0, buffer many proteolytic fragments were produced. On the addition of univalent cations in excess of 50 m m only two fragments, which had molecular weights of 49,000 and 52,000, were produced. When membranes were solubilized in the nonionic detergent Lubrol PX before trypsin treatment the pattern of polypeptide fragments produced was almost identical to that obtained in the absence of this detergent. From these results it was concluded that in the presence of 50 m m KCl the 100,000 molecular weight, Ca2+-activated adenosine triphosphatase A2 protein has only one region of its polypeptide chain which is accessible to trypsin. Although the molecular weights of the sarcoplasmic reticulum Ca2+-activated ATPase and erythrocyte Na+, K+-activated adenosine triphosphatase are very similar, the results reported here indicate that these two enzymes have different conformations in the two membranes." @default.
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- W1987550340 date "1974-03-01" @default.
- W1987550340 modified "2023-10-15" @default.
- W1987550340 title "Effect of trypsin on the proteins of skeletal muscle sarcoplasmic reticulum" @default.
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- W1987550340 doi "https://doi.org/10.1016/0003-9861(74)90237-9" @default.
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