Association of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase The biochemical and electron-microscopic evidence

Maks V. Sukhodolets; Vladimir I. Muronetz; Valery L. Tsuprun; Alla S. Kaftanova; Natalia K. Nagradova

doi:10.1016/0014-5793(88)80248-5

Association of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase The biochemical and electron-microscopic evidence

Maks V. Sukhodolets, Vladimir I. Muronetz, Valery L. Tsuprun, Alla S. Kaftanova, Natalia K. Nagradova

Otolaryngology

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble 3-phosphoglycerate kinase. The strength of the association appeared to depend upon the functional state of both enzymes. The holoform of the dehydrogenase exhibited a lower affinity for the kinase than the enzyme-3-phosphoglycerol·NADH complex. The substrate-free 3-phosphoglycerate kinase associated much stronger with the acylated dehydrogenase than the kinase in complex with 1,3-diphosphoglycerate. Electron-microscopic evidence for the association of the soluble acyl-glyceraldehyde-3-phosphate dehydrogenase·NADH complex and 3-phosphoglycerate kinase was also obtained.

Original language	English (US)
Pages (from-to)	161-166
Number of pages	6
Journal	FEBS Letters
Volume	238
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(88)80248-5
State	Published - Sep 26 1988

Keywords

3-Phosphoglycerate kinase
Bienzyme complex
Electron-microscopic study
Glyceraldehyde-3-phosphate dehydrogenase

Publisher link

10.1016/0014-5793(88)80248-5

Find It

Find It at U of M Libraries

Cite this

@article{482a1cee6fc34a2d9c379b41caef8645,

title = "Association of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase The biochemical and electron-microscopic evidence",

abstract = "Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble 3-phosphoglycerate kinase. The strength of the association appeared to depend upon the functional state of both enzymes. The holoform of the dehydrogenase exhibited a lower affinity for the kinase than the enzyme-3-phosphoglycerol·NADH complex. The substrate-free 3-phosphoglycerate kinase associated much stronger with the acylated dehydrogenase than the kinase in complex with 1,3-diphosphoglycerate. Electron-microscopic evidence for the association of the soluble acyl-glyceraldehyde-3-phosphate dehydrogenase·NADH complex and 3-phosphoglycerate kinase was also obtained.",

keywords = "3-Phosphoglycerate kinase, Bienzyme complex, Electron-microscopic study, Glyceraldehyde-3-phosphate dehydrogenase",

author = "Sukhodolets, {Maks V.} and Muronetz, {Vladimir I.} and Tsuprun, {Valery L.} and Kaftanova, {Alla S.} and Nagradova, {Natalia K.}",

year = "1988",

month = sep,

day = "26",

doi = "10.1016/0014-5793(88)80248-5",

language = "English (US)",

volume = "238",

pages = "161--166",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - Association of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase The biochemical and electron-microscopic evidence

AU - Sukhodolets, Maks V.

AU - Muronetz, Vladimir I.

AU - Tsuprun, Valery L.

AU - Kaftanova, Alla S.

AU - Nagradova, Natalia K.

PY - 1988/9/26

Y1 - 1988/9/26

N2 - Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble 3-phosphoglycerate kinase. The strength of the association appeared to depend upon the functional state of both enzymes. The holoform of the dehydrogenase exhibited a lower affinity for the kinase than the enzyme-3-phosphoglycerol·NADH complex. The substrate-free 3-phosphoglycerate kinase associated much stronger with the acylated dehydrogenase than the kinase in complex with 1,3-diphosphoglycerate. Electron-microscopic evidence for the association of the soluble acyl-glyceraldehyde-3-phosphate dehydrogenase·NADH complex and 3-phosphoglycerate kinase was also obtained.

AB - Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble 3-phosphoglycerate kinase. The strength of the association appeared to depend upon the functional state of both enzymes. The holoform of the dehydrogenase exhibited a lower affinity for the kinase than the enzyme-3-phosphoglycerol·NADH complex. The substrate-free 3-phosphoglycerate kinase associated much stronger with the acylated dehydrogenase than the kinase in complex with 1,3-diphosphoglycerate. Electron-microscopic evidence for the association of the soluble acyl-glyceraldehyde-3-phosphate dehydrogenase·NADH complex and 3-phosphoglycerate kinase was also obtained.

KW - 3-Phosphoglycerate kinase

KW - Bienzyme complex

KW - Electron-microscopic study

KW - Glyceraldehyde-3-phosphate dehydrogenase

UR - http://www.scopus.com/inward/record.url?scp=0023735762&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023735762&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(88)80248-5

DO - 10.1016/0014-5793(88)80248-5

M3 - Article

C2 - 3169248

AN - SCOPUS:0023735762

SN - 0014-5793

VL - 238

SP - 161

EP - 166

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Association of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase The biochemical and electron-microscopic evidence

Abstract

Keywords

Publisher link

Find It

Other files and links

Fingerprint

Cite this