Affinity chromatographic preparation of arterial heavy meromyosin subfragment-1 |
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Authors: | R Lamed Ulrike Mrwa |
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Institution: | (1) II. Physiologisches Institut der Universität Heidelberg, Im Neuenheimer Feld 326, D-69 Heidelberg 1, (German Federal Republic, BRD);(2) Present address: Weizmann Institut of Science, Rehovot |
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Abstract: | Summary Heavy meromyosin subfragment-1 (HMM S-1) was prepared by papain digestion of arterial myosin or actomyosin and was purified by agarose-ATP affinity chromatography. Proteolysis of crude arterial myosin suspensions was preceded by solubilization. HMM-S-1 thus obtained consisted mainly of a 90,000 dalton polypeptide and fully retained the K+- and Ca2+-ATPase of the parent myosin. Its affinity to agarose-ATP was comparable to that of skeletal muscle HMM S-1.The support of this work by an EMBO short time fellowship (to R. L.) and by the Deutsche Forschungsgemeinschaft (No. SFB 90, B 7) and the excellent technical assistance byM. Troschka andC. Köhler are gratefully acknowledged. |
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