HUMAN CLASS-III ALCOHOL-DEHYDROGENASE GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE

Kaiser, R; Holmquist, B; Vallee, BL; Jornvall, H

HERO ID

1578938

Reference Type

Journal Article

Year

1991

PMID

2054065

HERO ID 1578938
In Press No
Year 1991
Title HUMAN CLASS-III ALCOHOL-DEHYDROGENASE GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE
Authors Kaiser, R; Holmquist, B; Vallee, BL; Jornvall, H
Journal Journal of Protein Chemistry
Volume 10
Issue 1
Page Numbers 69-73
Abstract The class III human liver alcohol dehydrogenase, identical to glutathione-dependent formal-dehyde dehydrogenase, separates electrophoretically into a major anodic form (chi-1) of known structure, and at least one minor, also anodic but a slightly faster migrating form (chi-2). The primary structure of the minor form isolated by ion-exchange chromatography has now been determined. Results reveal an amino acid sequence identical to that of the major form, suggesting that the two derive from the same translation product, with the minor form modified chemically in a manner not detectable by sequence analysis. This pattern resembles that for the classical alcohol dehydrogenase (class I). Hence, the chi-1/chi-2 multiplicity does not add further primary forms to the complex alcohol dehydrogenase system but shows the presence of modified forms also in class III.
Doi 10.1007/BF01024657
Pmid 2054065
Wosid WOS:A1991FG06100008
Is Certified Translation No
Dupe Override No
Comments Source: Web of Science WOS:A1991FG06100008
Is Public Yes
Keyword AMINO ACID SEQUENCE; POST TRANSLATIONAL MODIFICATION; PEPTIDE ANALYSIS; ISOZYMES; HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY