Evidence for selenocysteine in ovine tissue organelles.

Abstract:

:Subcellular fractions were prepared by differential centrifugation from heart and liver of a lamb labeled with 75Se-selenite. Crude fractions of nuclei, mitochondria, and microsomes from both tissues were solubilized with sodium dodecyl sulfate and chromatographed on columns of sephacryl S-200. A low molecular weight (MW) 75Se labeled cardiac cytosol protein (approximately 10,000 daltons) was partially purified by gel filtration chromatography. The major 75Se peaks from the sephacryl columns and the low MW cardiac protein were hydrolyzed in HCl under an inert atmosphere. When chromatographed on an amino acid analysis column, 75Se from each hydrolysate chromatographed in the identical position of 2,7-diamino-4-thia-5-selenaoctanedioic acid, the mixed oxidized dimer of cysteine and selenocysteine. The low MW cardiac protein was reacted with chloroacetate after reduction with borohydride. 75Se from a hydrolysate of this derivatized protein eluted in the same position as Se-carboxymethylselenocysteine on the amino acid analysis column. Thus, selenocysteine appears to be the predominant form of selenium in ovine heart and liver.

journal_name

J Inorg Biochem

authors

Beilstein MA,Tripp MJ,Whanger PD

doi

10.1016/s0162-0134(00)80237-8

subject

Has Abstract

pub_date

1981-12-01 00:00:00

pages

339-47

issue

4

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(00)80237-8

journal_volume

15

pub_type

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