J. Biochem, 1988, Vol. 103, No. 4 688-692
© 1988 Japanese Biochemical Society
research-article |
Subunit Structures of Three Human Myeloperoxidases1
*Research Institute for Food Science, Kyoto University Uji, Kyoto 611
** Green Cross Co. Joto-ku, Osaka, Osaka 534
2To whom correspondence should be addressed.
The heavy and the light subunits of human myeloperoxidase (donor: H2O2 oxidoreductase [EC 1.11.1.7 [EC] ]) I, II, and III were isolated from the reduced and S-carboxymethylated enzymes. These three enzymes have the same terminal amino acid sequences and similar chemical compositions in both subunits. The NH2-terminal sequences of the heavy and light subunits were determined to be Val-Asn-Cys-Glu-Thr- and Thr-Cys-Pro-Glu-Gln-, respectively; a heterogeneity was observed in the NH2-termini of the latter subunits for the three enzymes. As for COOH-termini, the sequences -(Asn, 2 Leu, Ala, Ser, Trp)-Arg-Glu-Ala and -Ala-Arg were obtained for the heavy and the light subunits, respectively. The heavy subunits contained 8–10 mol/mol of glucosamine. On the basis of these results and the amino acid sequence deduced from cDNA clones, the heavy subunits probably correspond to amino acids 279–744 and the light subunits to amino acids (164–167)-272. For the heavy subunits, Ser-745, which was predicted as the COOH-terminal amino acid from the nucleotide sequence, was removed. The light subunits were also processed at their COOH-termini by 6 residues. Four or five high mannose type carbohydrate chains were attached to the heavy subunits.
1 This work was supported in part by a Grant-in-Aid for Scientific Research (No. 61470128) from the Ministry of Education, Science and Culture of Japan.