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. 1982 Oct 25;10(20):6511–6519. doi: 10.1093/nar/10.20.6511

Purification and properties of the Hpa I methylase.

O J Yoo, P Dwyer-Hallquist, K L Agarwal
PMCID: PMC326940  PMID: 6983681

Abstract

The purification and catalytic properties of the homogeneous Hpa I methylase is described. The enzyme exists as a single polypeptide chain with a molecular weight of 37,000 +/- 2,000 was shown by sedimentation equilibrium and polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The Hpa I methylase transfers methyl groups of S-adenosylmethionine to adenine present in the recognition sequence d(G-T-T-A-A*-C), A* is the N6 methyl adenosine. An average of 2.1 methyl groups per recognition site are transferred by the Hpa I methylase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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