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Article

Purification and properties of two forms of ATP sulfurylase from Euglena.

Biochimica et biophysica acta - 30 May 1991

Li J J, Saidha T, Schiff J A

Abstract excerpt

Two forms of ATP sulfurylase have been purified to homogeneity from mitochondria (ATPSm) and cells (ATPSc) of Euglena gracilis Klebs var. bacillaris Cori (aplastidic mutant W10BSmL). Both forms are monomeric, ATPSc is 52.3 kDa and ATPSm is 55 kDa. The pI is 7.9 for ATPSc and 5.8 for ATPSm. Therefore, ATPSm binds to DEAE-cellulose at pH 7.4; ATPSc does not. After cleavage by CNBr, the two forms of ATP sulfurylase...

Topics

Animals
Electrophoresis, Polyacrylamide Gel
Euglena gracilis
Hydrogen-Ion Concentration
Isoenzymes
Mitochondria
Molybdenum
Mutation
Sulfate Adenylyltransferase
Sulfates

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PMID: 1904773
DOI: 10.1016/0167-4838(91)90094-g

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1904773-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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