Immobilized dimers of D‐glyceraldehyde‐3‐phosphate dehydrogenase

Immobilized d‐glyceraldehyde‐3‐phosphate dehydrogenase can exist as a trimer

“…To evaluate the contribution of various types of intersubunit contacts to site-site interactions in the oligomer, a comparative study of enzyme species differing in the number of subunits (tetramer, trimer, dimer and monomer) seems attractive. Using the technique of matrix immobilization, we have prepared catalytically active monomeric [3] and dimeric [4] forms of the dehydrogenase; the latter enzyme species manifested the phenomenon of half-of-the-sites reactivity [5,6] and the non-equivalence of NAD'-binding sites [ 71.…”

Effect of Specific Antibodies on d-Glyceraldehyde-3-Phosphate Dehydrogenase

“…In addition to the above-mentioned limited modification of -SH groups of the dehydrogenase, another example of enzyme inactivation not leading to any change in immunochemical properties is the ADPinduced inactivation and dissociation [18]. We have shown that 82% loss of activity after incubation in the presence of ADP had no influence on the quantitative precipitin curve of the dehydrogenase.…”

“…To reveal the effect of Fab fragments on the conformation of the dehydrogenase, they were tested for a protective effect against two types of inactivation, caused by different agents and supposed to involve different structural changes. Both of them, namely, NaC1-induced cold inactivation [ 101 and ADP-induced inactivation [18] arc fully reversible and are accompanied by dissociation into subunits.…”

“…Fig.4A shows a typical inactivation pattern of glyceraldehyde-3-phosphate dehydrogenase from rat skeletal muscle in the presence of ADP. Previously we have demonstrated that nucleotide-induced inactivation involves dissociation of the enzyme into dimers; it may be completely reversed by removiing ADP with gel filtration [18]. To compare the efiect of Fab fragments on the inactivation of glyceraldehyde-3-phosphate dehydrogenase induced by different factors, the experiment illustrated in Fig.4B was carried out.…”

Immobilization of Enzymes: An Approach to Fundamental Studies in Biochemistry

“…It has been demonstrated (133) that the loss of activity of D-glyceraldehyde-3-phosphate dehydrogenase on interaction with AMP and ADP is due to conformational changes rather than to dissociation into dimers. If a trimer forms as an intermediate during the reassociation of this enzyme, the intermonomer interactions in it are energetically unequal (the trimeric particle consists of a dimer, in which the monomers are firmly bound, and a third monomer that interacts with the other two in a weaker manner) (135).…”