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J Biol Chem, Vol. 273, Issue 46, 30669-30674, November 13, 1998

Betaine-homocysteine Methyltransferase Is a Developmentally Regulated Enzyme Crystallin in Rhesus Monkey Lens

P. Vasantha Rao, Timothy A. Garrow^¶, Faith John, Donita Garland, Norman S. Millian^¶, and J. Samuel Zigler Jr.

From the  Laboratory of Mechanisms of Ocular Diseases, National Eye Institute, National Institutes of Health, Bethesda, Maryland 20892-2735 and ^¶ Department of Food Science and Human Nutrition, University of Illinois, Urbana, Illinois 61801.

We describe herein the characterization of a major 45-kDa protein from the soluble H-crystallin fraction of rhesus monkey (Macaca mulatta) lens. Based on partial peptide sequence, immunoreactivity, and enzymatic activity, this protein has been identified as betaine-homocysteine S-methyltransferase (BHMT: EC 2.1.1.5), an enzyme that catalyzes the methylation of homocysteine using either betaine or thetins as methyl donors. This protein was found to be expressed abundantly in the nuclear region of the monkey lens, reaching ~10% of the total nuclear protein, but was barely detectable in the epithelium and cortex regions of the lens. Because the nucleus represents the early embryonic and fetal stages of lens development, we infer that BHMT expression in the lens of the eye is developmentally regulated. By virtue of its high abundance, BHMT can be considered an enzyme crystallin (-crystallin). This is the first enzyme crystallin to be found in primate lenses.

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