Affinity chromatographic preparation of arterial heavy meromyosin subfragment-1

R. Lamed*, Ulrike Mrwa

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)1221-1222
Number of pages2
JournalExperientia
Volume32
Issue number9
DOIs
StatePublished - Sep 1976
Externally publishedYes

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