Literature DB >> 19873391

STUDIES ON THE ANOMALOUS VISCOSITY AND FLOW-BIREFRINGENCE OF PROTEIN SOLUTIONS : III. CHANGES IN THESE PROPERTIES OF MYOSIN SOLUTIONS IN RELATION TO ADENOSINETRIPHOSPHATE AND MUSCULAR CONTRACTION.

M Dainty1, A Kleinzeller, A S Lawrence, M Miall, J Needham, D M Needham, S C Shen.   

Abstract

1. An investigation of the physicochemical properties of myosin has been carried out. Prepared under standard conditions, the ratio of flow-birefringence to protein concentration is uniform. The effect of electrolytes, pH, and urea on the flow-birefringence and viscosity (relative and anomalous) of myosin has been examined. 2. Decrease or abolition of flow-birefringence does not necessarily imply far reaching denaturation, since such effects can be reversed by a variety of means. 3. When a myosin solution is treated with adenosinetriphosphate, its flow-birefringence is decreased (average 48 per cent), its anomalous viscosity is retained, and its relative viscosity is decreased (average 14 per cent). The full effect of adenosinetriphosphate is obtained at 0.004 M; a molarity very much less than that of other substances which decrease the flow-birefringence of myosin. 4. The changes in the physicochemical properties of myosin brought about by adenosinetriphosphate are spontaneously reversible, and are connected with the enzymatic action of the protein as adenosinetriphosphatase. 5. Effects similar to those of adenosinetriphosphate on the physicochemical properties of purified myosin have been obtained so far only with inosinetriphosphate. 6. Inorganic phosphate is split off by myosin from inosinetriphosphate as well as from adenosinetriphosphate. Inorganic triphosphate is split by 1 to 2 per cent solution of three times precipitated myosin. 7. Adenosinediphosphate and inorganic triphosphate act as competitive inhibitors with adenosinetriphosphate, blocking the fall of flow-birefringence. 8. The implications of the results, and the conception of active enzymic groups attached to proteins participating in cell structure, whether contractile or non-contractile, are discussed in relation to present views on muscle physiology and other biological problems.

Entities:  

Year:  1944        PMID: 19873391      PMCID: PMC2238015          DOI: 10.1085/jgp.27.4.355

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  6 in total

1.  [The contractile proteins in the myometrium].

Authors:  H SCHWALM; K CRETIUS; G LANGE
Journal:  Arch Gynakol       Date:  1955

2.  Between biochemists and embryologists -- the biochemical study of embryonic induction in the 1930s.

Authors:  Rony Armon
Journal:  J Hist Biol       Date:  2012       Impact factor: 1.326

3.  Reconstitution of contractile actomyosin arrays.

Authors:  Michael Murrell; Todd Thoresen; Margaret Gardel
Journal:  Methods Enzymol       Date:  2014       Impact factor: 1.600

4.  Muscular contraction.

Authors:  A F Huxley
Journal:  J Physiol       Date:  1974-11       Impact factor: 5.182

5.  Histochemical method for the demonstration of myosin adenosine triphosphatase in muscle tissues.

Authors:  A E Meijer
Journal:  Histochemie       Date:  1970

6.  The early history of the biochemistry of muscle contraction.

Authors:  Andrew G Szent-Györgyi
Journal:  J Gen Physiol       Date:  2004-06       Impact factor: 4.086

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.