Appendix. Purification, molecular weight, and NH2-terminal sequence of cystathionine gamma-synthase of Escherichia coli.

The Journal of biological chemistry ·Vol. 258 ·No. 24 ·1983-12-25 ·Pages 14872-3

Tran SV, Schaeffer E, Bertrand O, Mariuzza R, Ferrara P

Abstract

The cystathionine gamma-synthase of Escherichia coli has been purified to homogeneity. It is a tetramer (Mr = 160,000) composed of identical subunits (Mr approximately 40,000). We have determined its amino acid terminal sequence and thus localized the starting codon of the metB structural gene.

MeSH Terms

Amino Acid Sequence Cystathionine beta-Synthase/analysis,isolation & purification Escherichia coli/enzymology Hydro-Lyases/isolation & purification Macromolecular Substances Molecular Weight

Chemicals

Macromolecular Substances Hydro-Lyases Cystathionine beta-Synthase

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Tran S V

Schaeffer E

Bertrand O

Mariuzza R

Ferrara P

Article Info

Journal

The Journal of biological chemistry

Abbr.

J Biol Chem

ISSN

0021-9258

Published

1983-12-25

Pages

14872-3

Language

English

Region

United States

NLM ID

2985121R

Subset

External Links

PubMed source View journal details

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Appendix. Purification, molecular weight, and NH2-terminal sequence of cystathionine gamma-synthase of Escherichia coli.

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