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Purification and characterization of protein methylase II from Helicobacter pylori.

Authors
Kim, YM; Ahn, SH; Seo, DW; Kim, YK; Han, JW; Hong, S; Kim, S; Paik, WK; Lee, HW
Citation
FEMS microbiology letters, 195(1):53-58, 2001
Journal Title
FEMS microbiology letters
ISSN
0378-10971574-6968
Abstract
Protein methylase II (AdoMet:protein-carboxyl O-methyltransferase, EC 2.1.1.24) was identified and purified 115-fold from Helicobacter pylori through Q-Sepharose ion exchange column, AdoHcy-Sepharose 4B column, and Superdex 200 HR column chromatography using FPLC. The purified preparation showed two protein bands of about 78 kDa and 29 kDa molecular mass on SDS-PAGE. On non-denaturing gel electrophoresis, the enzyme migrated as a single band with a molecular mass of 410 kDa. In addition, MALDI-TOF-MS analysis and Superdex 200 HR column chromatography of the purified enzyme showed a major mass signal with molecular mass values of 425 kDa and 430 kDa, respectively. Therefore, the above results led us to suggest that protein methylase II purified from H. pylori is composed of four heterodimers with 425 kDa (4x(78+29)=428 kDa). This magnitude of molecular mass is unusual for protein methylases II so far reported. The enzyme has an optimal pH of 6.0, a K(m) value of 5.0x10(-6) M for S-adenosyl-L-methionine and a V(max) of 205 pmol methyl-(14)C transferred min(-1) mg(-1) protein.
MeSH terms
Amino Acid SequenceHelicobacter Infections/microbiologyHelicobacter pylori/enzymology*HumansMolecular Sequence DataProtein O-Methyltransferase/chemistryProtein O-Methyltransferase/isolation & purification*Protein O-Methyltransferase/metabolism*Substrate Specificity
PMID
11166995
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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