The change of erythrocyte shape following action of different substances altering Mg++-dependent ATPase activity (actomyosin-like protein)
Author:
Publisher
Springer Science and Business Media LLC
Subject
Hematology,General Medicine,Hematology
Link
http://link.springer.com/content/pdf/10.1007/BF00999859.pdf
Reference19 articles.
1. Avissar N., de Vries A., Ben-Shaul Y. & Cohen I.: Actin-activated ATPase from human erythrocytes.Biochim. biophys. Acta 375, 35 (1975).
2. Drickamer L. K.: Red cell membrane contains 3 different adenosine triphosphatases.J. Biol. Cbem. 250, 1952 (1975).
3. Gárdos G., Szász I. & Árky I.: Structure and function of erythrocytes.Acta biochim. biophys. Acad. Sci. Hung. 1, 253 (1966).
4. Kirkpatrick F. H., Woods G. M. & La Celle P. L.: Absence of one component of spectrin adenosine triphosphatase in hereditary spherocytosis.Blood 46, 945 (1975).
5. Laris P. C. & Letchworth P. E.: Characteristics of an adenosine triphosphatase in erythrocyte membrane stimulated by 2.4-Dinitrophenol.J. Cell Physiol. 69; 143 (1967).
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Erythrocyte protein 4.1 binds and regulates myosin.;Proceedings of the National Academy of Sciences;1989-12-01
2. Is there any connection between heat inactivation of spectrin-dependent ATPase and loss of smooth biconcave shape of red cells?;Cell Biochemistry and Function;1983-10
3. ATPases: Common and unique features within a group of enzymes;Folia Microbiologica;1982-05
4. The role of Mg++-ATPase (actomyosin-like protein) in maintaining the biconcave shape of erythrocytes;Blut;1977-10
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