PMID: 109446Jul 10, 1979

Subunit structure of higher plant glyceraldehyde-3-phosphate dehydrogenases (EC 1.2.1.12 and EC 1.2.1.13).

The Journal of Biological Chemistry
R Cerff, S E Chambers

Abstract

In a previous publication (Cerff, R. (1979) Eur. J. Biochem., 94, 243--247) we demonstrated that chloroplast NADP-linked glyceraldehyde-3-P dehydrogenase (EC 1.2.1.13) from higher plants consists of two separate isoenzymes with apparent subunit compositions A2B2 (isoenzyme 1) and A4 (isoenzyme 2), where Subunits A and B are distinguished by slightly different molecular weights (A smaller than or approximately to B). In the present study we compare isoenzymes 1 and 2 from Sinapis alba and Hordeum vulgare on the basis of antigenic cross-reactivity, tryptic peptides, and amino acid composition. Isoenzymes 1 and 2 show immunochemical identity. They also have very similar tryptic peptide maps and amino acid compositions. This strongly suggests that Subunits A and B of the NADP-linked enzyme are very similar in primary sequence. As opposed to this, cytoplasmic NAD-specific glyceraldehyde-3-P dehydrogenase (EC 1.2.1.12) does not cross-react with antisera raised against the NADP-linked enzyme. Furthermore, tryptic peptide maps of the NAD-specific enzyme show little or no similarity with those of the NADP-linked enzyme. This indicates that the subunits of the NADP-linked enzyme and the subunit of the NAD-specific enzyme are different pr...Continue Reading

Related Concepts

Amino Acids
Hordeum vulgare
Immunodiffusion Measurement
Glyceraldehyde-3-Phosphate Dehydrogenases
Alloenzymes
Molecular Weight
Peptide Fragments
Plants
Species Specificity
Trypure

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