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- W2038634081 abstract "The molecular structure of the spleen green heme protein was reinvestigated by gel‐permeation, SDS‐polyacrylamide gel electrophoresis, and amino acid analysis. The results showed that the enzyme is a tetramer ( M r 1.5 × 10 5 ) with two heavy subunits ( M r 6 × 10 4 with a single prosthetic group per subunit) and two light subunits ( M r 1.5 × 10 4 ), and that the tetramer structure is maintained by disulfide bond(s). The amino acid composition of the spleen green heme protein is similar to that of granulocyte myeloperoxidase. The present results contradict the data of Davis and Averill [(1981) J. Biol. Chem. 256, 5992‐5996], who reported the enzyme as a monomeric peroxidase with an M r of 57 000." @default.
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- W2038634081 date "1986-07-07" @default.
- W2038634081 modified "2023-10-14" @default.
- W2038634081 title "On the analogy in the structure of the spleen green heme protein and granulocyte myeloperoxidase" @default.
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- W2038634081 doi "https://doi.org/10.1016/0014-5793(86)80695-0" @default.
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