biochemist-in-chief (首席生物化學家)

Dr. Alton Meister, biochemist-in-chief (首席生物化學家)

The Chemistry of Glutathione: the Work of Alton Meister [2007](IR93)
Source:

http://www.jbc.org/content/282/38/e30.full

September 21, 2007 The Journal of Biological Chemistry, 282, e30.

Classic Article
Regulation of Gamma-glutamyL-cysteine Synthetase by Nonallosteric Feedback Inhibition by Glutathione (Richman, P. G., and Meister, A. (1975) J. Biol. Chem. 250, 1422–1426)

The Chemistry of Glutathione: the Work of Alton Meister
Nicole Kresge, Robert D. Simoni and Robert L. Hill

Regulation of Gamma-glutamyL-cysteine Synthetase by Nonallosteric Feedback Inhibition by Glutathione (Richman, P. G., and Meister, A. (1975) J. Biol. Chem. 250, 1422–1426)

Alton Meister (1922–1995) was born in New York City. He earned his B.S. from Harvard University in 1942 and his M.D. from Cornell University Medical College in New York in 1945. He then went to the National Cancer Institute at the National Institutes of Health and remained there until 1955 when he became chairman of the biochemistry department at the Tufts University School of Medicine. In 1967 Meister returned to the Cornell University Medical College and served as chairman of the college's biochemistry department until 1995. He was also biochemist-in-chief at New York Hospital from 1971 to 1995.


Dr. Alton Meister

Meister spent much of his career studying the chemistry of glutathione, a ubiquitous compound that protects cells from oxidation by absorbing oxygen. He had a suspicion (懷疑) that the compound might play an important role (扮演一個重要的角色)in the body's immune system (人體的免疫系統). This suspicion (懷疑) was confirmed (確認) when Meister observed (觀察到) that people infected (感染) with the AIDS (愛滋病) virus had exceptionally low levels of glutathione. Later, he found that glutathione can dramatically block the spread of the AIDS virus (可以戲劇性地阻止愛滋病病毒的蔓延) in vitro (在體外) and that the more glutathione that was used, the greater the effect. As a result, Meister helped transform glutathione into a drug that has shown some initial promise in reducing the growth of the AIDS virus (愛滋病病毒).

The Journal of Biological Chemistry (JBC) Classic reprinted here reports Meister's discovery that glutathione regulates its own synthesis. Glutathione is synthesized from L-glutamate and L-cysteine (【生物化學】半胱胺酸) via a γ-glutamyL-cysteine (【生物化學】半胱胺酸) intermediate. By examining the effect of glutathione and several related compounds on the activity of kidney γ-glutamy-cysteine synthetase, Meister was able to conclude that, “γ-glutamy-cysteine synthetase is inhibited by glutathione under conditions similar to those which prevail in vivo (在體內), thus strongly suggesting a physiologically significant feedback mechanism.”1

In addition to his work on glutathione, Meister authored the 2-volume Biochemistry of Amino Acids and was Editor of Advances in Enzymology and Associate Editor of the Journal of Biological Chemistry and the Annual Review of Biochemistry. He served on several Editorial Boards including those of the Journal of Biological Chemistry, Biochemistry, Methods in Biochemical Analysis, Biochimica et Biophysica Acta, and the Annual Review of Biochemistry. He was President of the American Society of Biological Chemists in 1977. Meister was a member of the National Academy of Sciences, the American Academy of Arts and Sciences, and the New York Academy of Sciences. He received many honors including the American Chemical Society's Paul-Lewis Award in enzyme chemistry (1954), the American Society of Biological Chemists' William C. Rose Award in biochemistry (1984), and the Chemical Industry Institute of Toxicology Founders' Award (1985).

Footnotes

1 More information about glutathione metabolism can be found in Meister's JBC Minireview (1).
The American Society for Biochemistry and Molecular Biology, Inc.

References

Meister, A. (1988) Glutathione metabolism and its selective modification. J. Biol. Chem. 263, 17205–17208 FREE Full Text

Related articles
P G Richman and A Meister
Regulation of Gamma-glutamyL-cysteine Synthetase by nonallosteric feedback inhibition by glutathione.
J. Biol. Chem. 1975 250: 1422-1426.