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Applied Biochemistry and
Microbiology, Vol. 35, ffo.
/. 1999, pp. 29-17. Translated from Prikladnayti Biokhimiya i
Mikrobialogiya, Vol. 35, No. 1,@  1999, pp. 34-42. Original Russian Text Copyright
© /999 hy Mosin, Skluclnev, Shvatz.

Incorporation of [2,3,4,5,6- 2H 5]Phenylalanine,

[3,5- 2H 2]Tyrosine,
and [2,4,5,6,7- 2H 5]Tryptophan

into the Bacteriorhodopsin Molecule of
Halobacterium halobium

O. V. Mosin*, D. A. Skladnev**, and V. I. Shvets*

Lotnonosov Moscow State Academy of Fine Chemical Technology, Moscow, 117571

** State
Center of Genetics and Selection of Industrial Microorganisms (GNU GENETICA),
Moscow, 113515 Russia

Received September 25, 1997

Abstract—Incorporation of
[2,3A5,6- 2H 5]phenylalanine, [3,5- 2H 2]tyrosine,
and [2,4,5,6,7- 2H 5]tryptophan into the
bacteriorhodopsin molecule followed by semipreparative isolation of
bacteriorhodopsin resulted in a yield of 8-10 mg per g bacterial biomass. This
method is based on the growth of the strain of halophilic bacteria Halobacterium
on a synthetic medium containing 2 H-labeled
aromatic ammo acids and fractionation of solubilized (in 0.5% sodium dodecyl
sulfate) protein by methanol, including purification of carotenoids. lip-ids, and
high-molecular-weight and low-molecular-weight compounds, as well as
gel-permeation chromatog-raphy on Sephadex G-200. Incorporation of 2H-labeled
amino acids was analyzed by electron impact mass spectrometry after
hydrolysis of the protein in 4 N Ba(OH) 2 and separation in the form
of methyl esters of /V-DNS derivatives of amino aids by re versed-phase
high-performance liquid chromatography.

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