A Unique Amino Acid Sequence around a Reactive Serine Residue in Peptidases from French Beans and Yeast
- 1 July 1967
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 104 (1), 5C
- https://doi.org/10.1042/bj1040005c
Abstract
The same sequence [glu-Ser-Val] is the site of reaction with DFP [di-isopropyl phosphorofluoridate] in phaseolain [the trivial name for the enzyme isolated from Phaseolus vulgaris] as the 3 main peptide bands representing this sequence are evident in the preparations examined. It is likely that the enzyme from brewer'' yeast (Felix Brouillet, 1966) that is inhibited by DFP would have the same sequence about a reactive serine residue as the enzyme in the preparation from baker''s yeast.This publication has 6 references indexed in Scilit:
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- Purification and properties of a proteolytic enzyme from French beansBiochemical Journal, 1965
- Reaction of Ficin with Diisopropylphosphorofluoridate. Evidence for a Contaminating Inhibitor*Biochemistry, 1965
- The amino acid sequence around the reactive serine residue of some proteolytic enzymesBiochemical Journal, 1960
- Amino-acid Sequence about the Reactive Serine of a Proteolytic Enzyme from Bacillus subtilisNature, 1960