Immobilized D-glyceraldehyde-3-phosphate dehydrogenase can exist as a trimer.

Content Provider	Semantic Scholar
Author	Ashmarina, Lyudmila Muronetz, Vladimir Nagradova, Natalya K.
Copyright Year	1981
Abstract	D-Glyceraldehyde-3-phosphate dehydrogenase (GAPD) is a tetrameric enzyme composed of identical subunits which exhibit marked cooperativity [ 1,2]. 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. The purpose of this investigation was to elaborate experimental conditions for preparation of an immobilized trimeric form of GAPD. We show that a trimer species of yeast GAPD is formed in the course of reassociation of a matrix-bound monomer and soluble dimers, which can be withdrawn from the solution and fixed in an immobilized state by means of interactions with a single subunit. Immobilized trimers served as a model for elucidation of the role of various types of subunit interactions in half-of-the-sites reactivity of yeast GAPD.
Starting Page	283S
Ending Page	283S
Page Count	1
File Format	PDF HTM / HTML
Alternate Webpage(s)	https://core.ac.uk/download/pdf/82419753.pdf
PubMed reference number	7023980v1
Volume Number	128
Issue Number	1
Journal	FEBS letters
Language	English
Access Restriction	Open
Subject Keyword	GAPDH gene Glyceraldehyde 3-Phosphate Glyceraldehyde-3-phosphate dehydrogenase Saccharomyces cerevisiae Yeast Two-Hybrid System Techniques monomer
Content Type	Text
Resource Type	Article