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Sawada, Hideo:
Ricerche immunologiche sull'actina di Helix pomatia L.
Atti della Accademia Nazionale dei Lincei. Classe di Scienze Fisiche, Matematiche e Naturali. Rendiconti Serie 8 39 (1965), fasc. n.5, p. 352-358, (Italian)
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Sunto

The results of the purification of actin from foot muscles of the snail Helix pomatia L. as well as those of the immunological and electrophoretic research carried out on the same protein are reported here. Actin was purified following Mommaerts's procedure which is based on the reversible transformation of G-actin into F-actin; the purity of the protein was tested by running it through Sephadex-200 columns. The presence of impurities was observed in the crude preparations by means of electrophoresis on starch gel, immunoelectrophoresis and immunodiffusion on microdishes. After purification, this foreign matter could no longer be detected. A comparative analysis was performed on actins from other species of Molluscs and from the striated muscles of the rabbit. The rabbit actin is immunologically different from that of the Gastropoda and the Lamellibranchia studied in the present investigation.
Referenze Bibliografiche
[1] ASAKURA S., Preparazione delle proteine della muscolatura (Actina). (In Giapponese) «Protein, Nucleic acid, Enzyme», 2, 282-286 (1957).
[2] BASTIDE P., Enzymes of Helix pomatia L., «Ann. Biol. Clin.», 12, 586-589 (1954), «Chemical Abstract», 49, 7765 b (1955).
[3] BOLOGNANI FANTIN A. M. e BOLOGNANI L., Dati biochimici e istochimici sulla mucinogenesi in Helix pomatia, «Istituto Lombardo (Rend. Sc.)», 98, 343-354 (1964).
[4] CARSTEN M. E. and MOMMAERTS W. F. H. M., A study of actin by means of starch gel electrophoresis, «Biochemistry», 2, 28-32 (1963).
[5] CARSTEN M. E. and KANTZ A. M., Actin: A comparative study, «Biochim. Biophys. Acta», 90, 534-541 (1964).
[6] CIGADA M., CITTERIO P., ORLANDI A., RANZI S. e TOSI L., Ricerche sulle proteine cellulari, «Istituto Lombardo (Rend. Sc.)», 82, 351-386 (1949).
[7] CIGADA M., CITTERIO P., RANZI S. e TOSI L., On the zoological specificity of myosin and actin, «Experientia», 4, 480-481 (1948).
[8] FURMINGER I. G. S., The antigenic constituents of myosin preparations, «Biochim. Biophys. Acta», 90, 521-523 (1964).
[9] KESZTYÜS L., NIKODÉMUSZ S. and SZILÁGYI T., Antigenic activity of myosin and actin, «Nature», 163, 136 (1949).
[10] KESZTYÜS L., NIKODÉMUSZ S. and SZILÁGYI T., Über die Artspezifität von actin, «Experientia», 6, 342-343 (1950).
[11] KRANS H. M. J., VAN HEIJK H. G. and WESTENBRINK H. G. K., Starch-Gel Electrophoresis and Ultracentrifugation of actin, «Biochim. Biophys. Acta», 65, 166-168 (1962).
[12] KRANS H. M. J., VAN HEIJK H. G. and WESTENBRINK H. G. K., A study of G-actin, «Biochim. Biophys. Acta», 100, 193-201 (1965).
[13] KUBIŠTA V., Flavones in Helix pomatia L., «Experientia», 6, 100 (1950).
[14] IRISAWA H. and IRISAWA A., Paper electrophoresis of the invertebrates body fluid protein, «J. Hiroshima Med. Ass.», 7, 436-438 (1954).
[15] LOWRY O. H., ROSEBROUGH N. J., FARR A. L. and RANDALL R. G., Protein measurement with the folin phenol reagent, «J. Biol. Chem.», 193, 265-275 (1951).
[16] MOMMAERTS W. F. H. M., Reversible polymerization and ultracentrifugal purification of actin, «J. Biol. Chem.», 188, 559-565 (1951).
[17] MOMMAERTS W. F. H. M., The molecular transformations of actin, «J. Biol. Chem.», 198, 445-457 (1952).
[18] MOMMAERTS W. F. H. M., Chemical investigation of muscular tissues, «Methods in Medical Research, Chicago the Year Book publishers, Inc.», 7, 1 (1958).
[19] POULIK M. D., Starch gel electrophoresis in a discontinuous system of buffers, «Nature», 180, 1477-1479 (1957).
[20] RANZI S., Alcune questioni sulle proteine protoplasmatiche, «Bollettino Società Italiana Biologia Sperimentale», 58, 487-511 (1952).
[21] SELBY C. C. and BEAR R. S., The structure of actin-rich filaments of muscles according to x-ray diffraction, «J. Biophysic Biochem. Cytol.», 2, 71-85 (1956).
[22] SMITHIES O., Zone electrophoresis in starch gel and its application to studies of serum proteins, «Advances in Protein Chemistry», 14, 56-113 (1959).
[23] TRAN VAN KY P., ROSE F. et LANDE F., L'étude immunoélectrophoretique de la structure antigénique des Mollusques est-elle susceptible de résoudre certaines difficultés de leur taxonomie?, «C. R. Acad. Sc. Paris», 255, 366-367 (1962).

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