Use of toluidine diisocyanide and glutaric dialdehyde in the conjugation of heavy meromyosin with light meromyosin

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Abstract

The fractions of digested myosin A were conjugated using toluidine diisocyanide and glutaric aldehyde as crosslinking agents. While helical content was relatively constant, the electrophoretic mobility, solubility, as well as ammonium sulfate precipitation of the conjugates were markedly different from those of the parent proteins.

Although the conjugates did not show superprecipitation at low ionic strength, they combined readily with actin and ATP at high ionic strength.

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Supported by NIH grant NB-03600-04.

2

Present address Department of Physiology, Woman's Medical College of Pennsylvania, Philadelphia, Pennsylvania.

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